High throughput glycan microarrays

ABSTRACT

The invention provides arrays of glycans for detecting entities that bind to glycans. In some embodiments, the arrays can be used to detect disease, blood types, antibodies, bacterial or viral infection, cancer, and the like. The invention also provides methods and kits for such detection. In another embodiment, the invention provides methods of preventing or treating disease in a mammal by administering to the mammal a composition that includes at least glycan.

This application is a continuation under 35 U.S.C. 111(a) ofInternational Application No. PCT/US2005/007370 filed Mar. 7, 2005 andpublished as WO 2005/088310 on Sep. 22, 2005, which claims benefit ofthe filing dates of U.S. Provisional Ser. No. 60/550,667, filed Mar. 5,2004, U.S. Provisional Ser. No. 60/558,598, filed Mar. 31, 2004, andU.S. Provisional Ser. No. 60/629,833, filed Nov. 19, 2004, the contentsof which applications and publication are incorporated herein byreference.

GOVERNMENT FUNDING

The invention described herein was made with United States Governmentsupport under Grant Number U54GM62116 awarded by the National Institutesof Health. The United States Government has certain rights in thisinvention.

FIELD OF THE INVENTION

The invention relates to glycan libraries, glycan arrays and methods forhigh throughput identification of the molecules that bind to varioustypes of glycans. The arrays and methods provided herein can be used forepitope identification, for detecting antibodies, for detecting disease,for drug discovery and as analytical tools. In another embodiment, theinvention provides glycan compositions useful for treating andprevention diseases associated with the production of those antibodies.These glycan compositions can be used to generate an immune responseagainst cancer cell epitopes, bacterial infections, viral infections andthe like.

BACKGROUND OF THE INVENTION

Glycans are typically the first and potentially the most importantinterface between cells and their environment. As vital constituents ofall living systems, glycans are involved in recognition, adherence,motility and signaling processes. There are at least three reasons whyglycans should be studied: (1) all cells in living organisms, andviruses, are coated with diverse types of glycans; (2) glycosylation isa form of post- or co-translational modification occurring in all livingorganisms; and (3) altered glycosylation is an indication of an earlyand possibly critical point in development of human pathologies. JunHirabayashi, Oligosaccharide microarrays for glycomics; 2003, Trends inBiotechnology.21 (4): 141-143; Sen-Itiroh Hakomori, Tumor-associatedcarbohydrate antigens defining tumor malignancy: Basis for developmentof and-cancer vaccines; in The Molecular Immunology of ComplexCarbohydrates-2 (Albert M Wu, ed., Kluwer Academic/Plenum, 2001). Thesecell-identifying glycosylated molecules include glycoproteins andglycolipids and are specifically recognized by variousglycan-recognition proteins, called ‘lectins.’ However, the enormouscomplexity of these interactions, and the lack of well-defined glycanlibraries and analytical methods have been major obstacles in thedevelopment of glycomics.

The development of nucleotide and protein microarrays has revolutionizedgenomic, gene expression and proteomic research. While the pace ofinnovation of these arrays has been explosive, the development of glycanmicroarrays has been relatively slow. One reason for this is that it hasbeen difficult to reliably immobilize populations of chemically andstructurally diverse glycans. Moreover, glycans are not readily amenableto analysis by many of the currently available molecular techniques(such as rapid sequencing and in vitro synthesis) that are routinelyapplied to nucleic acids and proteins. However, the use of glycan arrayscould expedite screening procedures, making detection of antibodies,disease, infection, transplant tissue rejection and cancer-relatedglycan epitopes simple and inexpensive.

Thus, new tools and procedures to expedite analysis of carbohydrateinteractions, to facilitate identification of antibodies and theepitopes they recognize, to permit early detection of disease andprovide new methods for discovering effective therapeutic agents.

SUMMARY OF THE INVENTION

The invention provides glycan libraries, glycan arrays (or microarrays)and methods for using such arrays to identify and analyze theinteractions that various types of glycans have with other molecules.These glycan libraries, glycan arrays and screening methods are usefulfor identifying which protein, receptor, antibody, nucleic acid or othermolecule or substance will bind to which glycan. The present glycanarrays permit many small samples of fluids or solutions to be screenedsimultaneously. The glycan arrays of the invention are reusable afterstripping with acidic, basic aqueous or organic washing steps. Thus, theglycan libraries and glycan arrays of the invention can be used forreceptor ligand characterization, anti-glycan antibody detection,diagnosis of disease, identification of carbohydrates on cell membranesand within subcellular components, antibody epitope identification,enzyme characterization and phage display library screening.

Thus, one aspect of the invention involves a library of glycans. Thelibraries of the invention include two or more glycans. Each glycan hasat least one sugar unit, typically at least two sugar units. The glycansof the invention include straight chain and branched oligosaccharides aswell as naturally occurring and synthetic glycans. Any type of sugarunit can be present in the glycans of the invention, including allose,altrose, arabinose, glucose, galactose, gulose, fucose, fructose, idose,lyxose, mannose, ribose, talose, xylose, neuraminic acid or other sugarunits. Such sugar units can have a variety of substituents. For example,substituents that can be present instead of, or in addition to, thesubstituents typically present on the sugar units include N-acetyl,N-acetylneuraminic acid, oxy (═O), sialic acid, sulfate (—SO₄ ⁻),phosphate (—PO₄ ⁻), lower alkoxy, lower alkanoyloxy, lower acyl, and/orlower alkanoylaminoalkyl. Fatty acids, lipids, amino acids, peptides andproteins can also be attached to the glycans of the invention. Thelibraries of the invention generally have many separate glycans, forexample, at least about 35 glycans, at least about 50 glycans, or atleast about 225 glycans.

In another embodiment, the invention provides an array of glycanmolecules comprising a solid support and a library of glycan molecules,wherein each glycan molecule is covalently attached to the solid supportvia amide linkage. In many embodiments, the array is a microarray.Arrays and microarrays of the invention include a solid support and amultitude of defined glycan probe locations on the solid support, eachglycan probe location defining a region of the solid support that hasmultiple copies of one type of glycan molecule attached thereto. Thesemicroarrays can have, for example, between about 2 to about 100,000different glycan probe locations, or between about 2 to about 10,000different glycan probe locations. The libraries of the invention cantherefore be attached to a solid support to form an array or amicroarray.

In another embodiment, the invention provides a method of identifyingwhether a test molecule or test substance can bind to a glycan presentin a library or on an array of the invention. The method involvescontacting the library or the array with the test molecule or testsubstance and observing whether the test molecule or test substancebinds to a glycan in the library or on the array.

In another embodiment, the invention provides a method of identifying towhich glycan a test molecule or test substance can bind, wherein theglycan is present in a library or on an array of the invention. Themethod involves contacting the library or the array with the testmolecule or test substance and observing to which glycan in the libraryor on the array the test molecule or test substance can bind.

In another embodiment, the invention provides a method making the arraysof the invention that involves derivatizing the solid support surface ofthe array with a trialkoxysilane bearing reactive moieties such asN-hydroxysuccinimide (NHS), amino (—NH₂), isothiocyanate (—NCS) orhydroxyl (—OH) to generate at least one derivatized glycan probelocation on the array, and contacting the derivatized probe locationwith a glycan solution containing a glycan with a linking moiety thatcan react with the reactive moieties on the derivatized surface tothereby provide the array. This density of glycans at each glycan probelocation can be modulated by varying the concentration of the glycansolution applied to the derivatized glycan probe location.

Another aspect of the invention is a composition comprising a carrierand an effective amount of at least one glycan molecule, wherein eachglycan molecule in the composition binds an antibody found in a patientwith a disease, and wherein serum from a patient without the disease hassubstantially no antibodies that bind any of the glycan molecules in thecomposition. Examples of diseases that can be treated with thecompositions of the invention include bacterial infections, viralinfections, inflammations, cancers, transplant rejection, autoimmunediseases or combinations thereof. These compositions can be formulatedfor immunization of a mammal. Alternatively, these compositions can beformulated in a food supplement. The compositions of the invention areuseful for treating and preventing diseases such as cancer, bacterialinfection, viral infection, inflammation, transplant rejection,autoimmune diseases and the like.

Another aspect of the invention is a method of detecting antibodies inbodily fluids of a patient. The method involves contacting a test sampleobtained from the patient with a glycan library or glycan array of theinvention, and observing whether antibodies in the test sample bind toglycans in the library or the array. According to one aspect of theinvention, the type of glycan bound by such antibodies is indicative ofthe presence of a distinctive disease, or the propensity to develop adistinctive disease in the patient. The binding pattern of test samplescan be compared to the binding of control samples from healthy patientsthat do not suffer from the disease in question. The test and controlsamples can, for example, be blood, serum, tissue, urine, saliva, milkor other samples. One convenient sample type for use in the invention isserum.

For example, patients with breast cancer have circulating antibodiesthat react with glycans such as ceruloplasmin, Neu5Acα2-6GalNAcα,certain T-antigens carrying various modifications, LNT-2 (a known ligandfor tumor-promoting Galectin-4; see Huflejt & Leffler (2004).Glycoconjugate J., 20: 247-255), Globo-H—, and GM1-antigens. GM1 is aglycan that includes the following carbohydrate structure:Gal-beta3-GalNAc-beta4-[Neu5Ac-alpha3]-Gal-beta4-Glc-beta. Sulfo-T is aT-antigen with sulfate residues, for example, Sulfo-T can include acarbohydrate of the following structure: Galβ3GalNAc. Globo-H is aglycan that includes the following carbohydrate structure:Fucose-alpha2-Gal-beta3-GalNAc-beta3-Gal-alpha4-Gal-beta4-Glc. LNT-2 isa glycan that includes the following carbohydrate structure:GlcNAc-beta3-Gal-beta4-Glc-beta. The presence of cancer can therefore bedetected with the present glycan arrays by detecting antibodies thatbind to these glycans. Moreover, cancer can be treated or prevented byadministering compositions of these cancer-specific antigens to boost animmune response against cancerous tissues.

In another example, neutralizing antibodies known to be specific for HIVwere found by use of the arrays and methods of the invention to bereactive with mannose-containing glycans, in particular Man8 glycans.Hence, HIV infection may be detected by detecting whether a patient hascirculating antibodies that bind to Man8 glycans. Moreover, HIVinfection can be treated or inhibited by administering Man8 glycans to asubject.

Another aspect of the invention is a method of detecting transplanttissue rejection in a transplant recipient comprising contacting a testsample from the transplant recipient with an array of glycans andobserving whether one or more glycans are bound by antibodies in thetest sample. The method can also be used to detect xenotransplant tissuerejection. Glycans specific for the transplanted or xenotranplantedtissue are used in glycan arrays to observe whether one or more glycansare bound by antibodies in the test sample. Examples of glycans that canbe used in an array for detecting transplant reject include any one ofGal-alpha3-Gal-beta (structure 33 of FIG. 7),Gal-alpha3-Gal-beta4-GlcNAc[alpha3-Fucose]-beta (structure 34 of FIG.7), Gal-alpha3-Gal-beta4-Glc-beta (structure 35 of FIG. 7),Gal-alpha3-Gal[alpha2-Fucose]-beta4-GlcNAc-beta (structure 36 of FIG.7), Gal-alpha3-Gal-beta4-GalAc-beta (structure 37 of FIG. 7),Gal-alpha3-GalAc-alpha (structure 38 of FIG. 7), Gal-alpha3-Gal-beta(structure 39 of FIG. 7), or Gal-beta4-GlcNAc[alpha3-Fucose]-beta(structure 65 in FIG. 7) or a combination thereof.

The glycans used on the arrays of the invention can therefore includeglycans that react with antibodies associated with particular disease orcondition. For example, antibodies that are produced in response tocancer, bacterial infection, viral infection, inflammation, transplantrejection, autoimmune diseases and the like can be detected using theglycan arrays of the invention.

Another aspect of the invention is an array or a microarray fordetecting breast cancer that includes a solid support and a multitude ofdefined glycan probe locations on the solid support, each glycan probelocation defining a region of the solid support that has multiple copiesof one type of glycan molecule attached thereto and wherein the glycansare attached to the microarray by a cleavable linker. These microarrayscan have, for example, between about 2 to about 100,000 different glycanprobe locations, or between about 2 to about 10,000 different glycanprobe locations. Glycans selected for use in the arrays or microarraysinclude those that react with antibodies associated with neoplasia insera of mammals with benign or pre-malignant tumors. Glycans such asceruloplasmin, Neu5Acα2-6GalNAcα, certain T-antigens, LNT-2, Globo-H—,and GM1 can be used in these types of arrays.

Another aspect of the invention is a kit comprising any of the arrays ofthe invention and instructions for using the array. In anotherembodiment, the invention provides a kit comprising the library ofglycans and instructions for making an array from the library ofglycans.

In another embodiment, the invention provides a method of identifyingwhether a patient or a mammal has a disease that includes contacting anarray or library of the invention with a test sample and observingwhether antibodies in the test sample bind to glycans that react withantibodies associated with the disease. For example, diseases that canbe detected include cancer, bacterial infection, viral infection,inflammation, transplant rejection, autoimmune diseases and the like.

In another embodiment, the invention provides a method of treating orpreventing a disease or condition in a mammal that comprisesadministering to the mammal a composition comprising an effective amountof at least one glycan molecule that binds antibodies associated withthe disease or condition. For example, diseases and conditions that canbe treated include cancer, bacterial infection, viral infection,inflammation, transplant rejection, autoimmune diseases and the like.

DESCRIPTION OF THE FIGURES

FIG. 1 illustrates covalent printing of a diverse glycan library onto anamino-reactive glass surface and image analysis using the microarraytechniques described herein. In some embodiments, anamino-functionalized glycan library is printed onto anN-hydroxysuccinimide (NHS) derivatized glass surface to form amicroarray of glycans where each glycan type is printed onto a knownglycan probe location.

FIG. 2 provides representative glycan structures that can be part of alibrary or used on an array of the invention. Many of these glycanstructures bind glycan binding proteins. The circular, square andtriangular symbols employed represent different sugar units; the meaningof these symbols is defined below the glycan listing. The followingabbreviations are used: Gal=galactose; Glc=glucose; Man=mannose;GalNAc=N-acetylgalactosamine; GlcNAc=N-Acetylglucosamine; Fuc=fucose;NeuAc=N-Acetylneuraminic acid; NeuGc=N-Glycolylneuraminic acid;KDN=2-Keto-3-deoxynananic acid; S═SO₃; SP1=(CH₂)₂—NH—; SP2=(CH₂)₃—NH—;SP3=(CH₂)₃—NH—; SP4=NH—(CO)(CH₂)₂—NH—; SP5=(CH₂)₄—NH—. Furtherinformation on the symbol nomenclature can be found at the website ofthe Consortium for Functional Glycomics(http://www.functionalglycomics.org). Other tables provided hereindescribe further glycan structures that can be used in the glycanlibraries and arrays of the invention. Further description of the typesof saccharides, saccharide derivatives and saccharide linkages employedcan be found in the tables and text provided herein.

FIG. 3A-C provides data illustrating printing optimization and thespecificity of selected plant lectins. FIG. 3A provides a graph relatingthe glycan concentration and length of printing time to the relativefluorescence of the signal detected from binding Concanavalin Aconjugated to fluorescinisothiocyanate (Con A-FITC). Optimized glycanconcentrations and printing times were determined by printing selectedmannose glycan structures and then detecting Con A binding thereto. Arepresentative mannose glycan (136, see FIG. 7) was printed at variousconcentrations (4 μM-500 μM) in replicates of eight at six differenttime points. FIG. 3B illustrates the binding specificity of Con A-FITCon the complete array of glycans whose structures are provided in FIG.7. As shown, Con A binds to mannose-containing glycans that can end withN-acetylglucosamine. FIG. 3C illustrates the binding specificity ofFITC-labeled Erythrina cristagalli (ECA-FITC) on the array of glycanswhose structures are provided in FIG. 7 and in Table 3 (glycans 1-200).As shown, Erythrina cristagalli binds togalactose-β4-N-acetylglucosamine-containing glycans that can end withfucose. The symbols employed for the depicted glycan structures are thesame as those described in FIG. 2.

FIG. 4A-D illustrate the specificity of mammalian glycan bindingproteins on a glycan array of the invention. FIG. 4A illustrates bindingby the C-type lectin, dendritic cell-specific ICAM-grabbing nonintegrin(DC-SIGN) to the glycan array whose structures are shown in FIG. 7. TheDC-SIGN was conjugated to a human Fc antibody fragment to permitdetection with a labeled anti-human IgG antibody preparation. Inparticular, the DC-SIGN-Fc chimera (30 μg/mL) was detected by secondarygoat anti-human-IgG-Alexa-488 antibody (10 μg/mL). As shown, DC-SIGNbound selectively to α1-2- and/or α1-3/4-fucosylated glycans as well asto Manα1-2-glycans. FIG. 4B illustrates binding by CD22, a member of thesialic acid-containing immunoglobulin superfamily of lectins (Siglec).CD22-Fc chimera (10 μg/mL) pre-complexed with secondary goatanti-human-IgG-Alexa-488 (5 μg/mL) and tertiary rabbitanti-goat-IgG-FITC (2.5 μg/mL) antibodies bound exclusively toNeu5Acα2-6Gal-glycans. FIG. 4C illustrates human galectin-4 binding tothe array of glycans. Human Galectin-4-Alexa488 (10 μg/mL) evaluatedwith glycans printed at 100 μM (100 μM) and at 10 μM (10 μM) boundpreferentially to blood group glycans.

FIG. 5A-C illustrate the specificity of various anti-carbohydrateantibodies on the glycan arrays of the invention. FIG. 5A shows thespecificity of an anti-CD15 antibody preparation for Lewis^(X) glycansthat contain N-acetylglucosamine-[α3(fucose)] [β4(galactose)]. Mouseanti-CD15-FITC monoclonal antibody (BD Biosciences Clone H198, 100tests) bound exclusively to Lewis^(X) glycans. FIG. 5B shows thespecificity of a human anti-HIV 2G12 monoclonal antibody for mannose-8and mannose-9 glycans. The anti-HIV 2G12 antibodies (30 μg/mL) werepre-complexed with goat anti-human-IgG-FITC (15 μg/mL). As shown theseantibodies bound to specific Manα1-2-glycans including the Man8 and Man9N-glycans. FIG. 5C shows the binding specificity of human serum for afew glycan types. Human serum from ten healthy individuals (1:25dilution) were individually bound to glycan arrays and detected bysubsequent overlay with monoclonal mouse anti-human-IgG-IgM-IgA-Biotinantibody (10 μg/mL) and Streptavidin-FITC (10 μg/mL) respectively.Results represent the mean and standard deviation for binding in all tenexperiments. Anti-carbohydrate antibodies present in the human serumbound to various blood group antigens as well as mannans and bacterialfragments.

FIG. 6A-C illustrate the specificity of various bacterial and viralglycan binding proteins for certain glycans in the arrays of theinvention. FIG. 6A shows the glycans bound by Cyanovirin-N, a bacterialglycan binding protein. Cyanovirin-N (30 μg/mL) binding was detectedwith secondary polyclonal rabbit anti-Cyanovirin-N (10 μg/mL) andtertiary anti-rabbit-IgG-FITC (10 μg/mL) antibodies. Cyanovirin-N boundvarious α1-2 mannosides. FIG. 6B illustrates the types of glycans boundby Influenza H3 hemagglutinin. Pure recombinant hemagglutinin (150μg/mL) that was derived from Duck/Ukraine/1/63 (H3/N7), waspre-complexed with mouse anti-HisTag-IgG-Alexa-488 (75 μg/mL) andanti-mouse-IgG-Alexa-488 (35 μg/mL). Incubation on the glycan array, ledto binding of the hemagglutinin exclusively to Neu5Acα2-3Gal-terminatingglycans. FIG. 6C shows that Influenza virus binds to the same type ofglycans as purified hemagglutinin. Intact influenza virus A/PuertoRico/8/34 (H1N1) was applied to the glycan array at a concentration of100 μg/ml in the presence of 10 μM of the neuraminidase inhibitoroseltamivir carboxylate. The virus bound a wide spectrum of sialosideswith both NeuAcα2-3Gal and NeuAcα2-6Gal sequences.

FIG. 7A-C provides a schematic diagram of glycan structures used in someof the libraries and glycan arrays of the invention. The symbolsemployed for the depicted glycan structures are the same as thosedescribed in FIG. 2, with a few additional symbols for sugar unitsdefined in the lower right hand corner of FIG. 7C. Glycans 1-200 shownin FIG. 7 correspond to glycans 1-200 provided in Table 3, where achemical name for each glycan is provided.

FIG. 8 provides a bar graph illustrating which glycans react withanti-carbohydrate antibodies found in sera of metastatic breast cancerpatients. The types of glycans to which the antibodies bound are definedby numbers on the x-axis, as follows: background (# 1, a negativecontrol), ceruloplasmin (#2), Neu5Gc(2-6)GalNAc (#3), Neu5Ac(2-6)GalNAc(#4), GMI (#5), Sulfo-T (#6), Globo-H (#7), LNT-2 (#8) and Rhamnose(#10, a positive control). Each bar clustered above the glycanidentified on the x-axis represents the relative fluorescence intensityof a given anti-glycan antibody in an individual patient. Red bars (bars1-9 in each cluster) represent the intensities observed for reaction ofmetastatic breast cancer patient sera with the glycans identified on thex-axis. Orange bars, which are the tenth bar in each cluster of bars,represent the average values for metastatic cancer patients 1-9. Yellowbars, which are the eleventh bars in each cluster or bars, represent theaverage values for non-metastatic breast cancer patients. Blue bars,which are the twelfth through twenty-first bars, represent the averagevalues of “healthy” individuals. Dark blue bars, which are twenty-secondbars in each cluster of bars, represent the average values for healthyindividuals.

FIG. 9 provides a bar graph illustrating the additive relativefluorescence levels of selected cancer-associated anti-glycan antibodiesin cancer (N=9) and non-cancer patients (N=10). The types of glycansthat react with these antibodies are shown with the number of patientswhose sera react with the indicated glycan type. The x-axis identifieswhether the serum was take from cancer patients or non-cancer patients.The inset provides a combined relative fluorescence levels for a groupof known cancer-associated T-antigens carrying various modifications inmetastatic breast cancer patients (1) and in “healthy” individuals (2).

FIG. 10 provides a bar graph illustrating the combined levels offluorescence (from FIG. 9) observed for the tumor associated anti-glycanantibodies in individual patient sera. The bars labeled “Cancer”represent the combined signals observed for each individual metastaticcancer patient. The bars labeled “Non-Cancer” represent the combinedsignal observed for each individual non-cancer patient.

FIG. 11A provides a structure for alpha-Gal, a glycan structure that isfound in several of the glycans that bind to antibodies from patientswho received transplanted porcine fetal pancreas islet-like cellclusters (the symbols used for this structure are defined herein, forexample, in FIG. 2 or 7).

FIG. 11B provides a structure for the LeX glycan (compound 65 in FIG.7), which is the glycan corresponding to compound 8 in the bar graph ofFIG. 11D.

FIG. 11C provides a structure for the alpha-Gal-LeX glycan (compound 34in FIG. 7), which is the glycan corresponding to compound 9 in the bargraph of FIG. 11D.

FIG. 11D provides a bar graph illustrating that certain circulatingantibodies, which are reactive with glycans, are present in diabeticpatients who received transplanted porcine fetal pancreas islet-likecell clusters. Serum was taken from these patients beforetransplantation and at 1 month after (t=1), 6 months after (t=2) and 12months after (t=3) transplantation. The bars represent the reactivity ofserum antibodies with glycans 33-39 (structures shown in FIG. 7) thatare identified as glycans 1-7, respectively, on the x-axis. The lighterbars (blue in the original) represent the reactivity of the identifiedglycan for antibodies in the patient's serum before transplantation. Thedarker bars (green in the original) represent the combined reactivitiesof the identified glycan for antibodies in the patient's serum at t=1-3after transplantation. Hence, an immune response directed againsttransplanted tissue can be detected using the glycan arrays of theinvention.

FIG. 12 illustrates that human saliva contains antibodies that binddiscrete types of glycans.

DETAILED DESCRIPTION OF THE INVENTION

The invention provides libraries and arrays of glycans that can be usedfor identifying which types of proteins, receptors, antibodies, lipids,nucleic acids, carbohydrates and other molecules and substances can bindto a given glycan structure.

The inventive libraries, arrays and methods have several advantages. Forexample, the arrays and methods of the invention provide highreproducible results. Moreover, the libraries and arrays of theinvention provide large numbers and varieties of glycans. For example,the libraries and arrays of the invention have at least two, at leastthree, at least ten, at least twenty, at least thirty five, at leastfifty, at least one hundred, or at least two hundred glycans. In someembodiments, the libraries and arrays of the invention have about 2 toabout 100,000, or about 2 to about 10,000, or about 2 to about 1,000, orabout 2 to 500 different glycans per array. Such large numbers ofglycans permit simultaneous assay of a multitude of glycan types.

As described herein, the present arrays have been used for successfullyscreening a variety of glycan binding proteins. Such experimentsdemonstrate that little degradation of the glycan occurs and only smallamounts of glycan binding proteins are consumed during a screeningassay. Hence, the arrays of the invention can be used for more than oneassay. The arrays and methods of the invention provide high signal tonoise ratios. The screening methods provided by the invention are fastand easy because they involve only one or a few steps. No surfacemodifications or blocking procedures are typically required during theassay procedures of the invention.

The composition of glycans on the arrays of the invention can be variedas needed by one of skill in the art. Many different glycoconjugates canbe incorporated into the arrays of the invention including, for example,naturally occurring or synthetic glycans, glycoproteins, glycopeptides,glycolipids, bacterial and plant cell wall glycans and the like.Immobilization procedures for attaching different glycans to the arraysof the invention are readily controlled to easily permit arrayconstruction.

Definitions

The following abbreviations may be used: α₁-AGP means alpha-acidglycoprotein; AF488 means AlexaFluour-488; CFG means Consortium forFunctional Glycomics; Con A means Concanavalin A; CVN meansCyanovirin-N; DC-SIGN means dendritic cell-specific ICAM-grabbingnonintegrin; ECA means Erythrina cristagalli; ELISA means enzyme-linkedimmunosorbent assay; FITC means Fluorescinisothiocyanate; GBP meansGlycan Binding Protein; HIV means human immunodeficiency virus; HA meansinfluenza hemagglutinin; NHS means N-hydroxysuccinimide; PBS meansphosphate buffered saline; SDS means sodium dodecyl sulfate; SEM meansstandard error of mean; and Siglec means sialic acid immunoglobulinsuperfamily lectins.

A “defined glycan probe location” as used herein is a predefined regionof a solid support to which a density of glycan molecules, all havingsimilar glycan structures, is attached. The terms “glycan region,” or“selected region”, or simply “region” are used interchangeably hereinfor the term defined glycan probe location. The defined glycan probelocation may have any convenient shape, for example, circular,rectangular, elliptical, wedge-shaped, and the like. In someembodiments, a defined glycan probe location and, therefore, the areaupon which each distinct glycan type or a distinct group of structurallyrelated glycans is attached is smaller than about 1 cm², or less than 1mm², or less than 0.5 mm². In some embodiments the glycan probelocations have an area less than about 10,000 μm² or less than 100 μm².The glycan molecules attached within each defined glycan probe locationare substantially identical. Additionally, multiple copies of eachglycan type are present within each defined glycan probe location. Thenumber of copies of each glycan types within each defined glycan probelocation can be in the thousands to the millions.

As used herein, the arrays of the invention have defined glycan probelocations, each with “one type of glycan molecule.” The “one type ofglycan molecule” employed can be a group of substantially structurallyidentical glycan molecules or a group of structurally similar glycanmolecules. There is no need for every glycan molecule within a definedglycan probe location to have an identical structure. In someembodiments, the glycans within a single defined glycan probe locationare structural isomers, have variable numbers of sugar units or arebranched in somewhat different ways. However, in general, the glycanswithin a defined glycan probe location have substantially the same typeof sugar units and/or approximately the same proportion of each type ofsugar unit. The types of substituents on the sugar units of the glycanswithin a defined glycan probe location are also substantially the same.

The term lectin refers to a molecule that interacts with, binds, orcrosslinks carbohydrates. The term galectin is an animal lectin.Galectins generally bind galactose-containing glycan.

As used herein a “patient” is a mammal or a bird. Such mammals and birdsinclude domesticated animals, farm animals, animals used in experiments,zoo animals and the like. For example, the patient can be a dog, cat,monkey, horse, rat, mouse, rabbit, goat, ape or human mammal. In otherembodiments, the animal is a bird such as a chicken, duck, goose or aturkey. In many embodiments, the patient is a human.

Some of the structural elements of the glycans described herein arereferenced in abbreviated form. Many of the abbreviations used areprovided in the Table 1. Moreover the glycans of the invention can haveany of the sugar units, monosaccharides or core structures provided inTable 1. TABLE 1 Long Short Trivial Name Monosaccharide/Core Code CodeD-Glcp D-Glucopyranose Glc G D-Galp D-Galactopyranose Gal A D-GlcpNAcN-Acetylglucopyranose GlcNAc GN D-GlcpN D-Glucosamine GlcN GQ D-GalpNAcN-Acetylgalactopyranose GalNAc AN D-GalpN D-Galactosamine GalN AQ D-ManpD-Mannopyranose Man M D-ManpNAc D-NJ-Acetylmannopyranose ManNAc MND-Neup5Ac N-Acetylneuraminic acid NeuAc NN D-Neu5GD-N-Glycolylneuraminic acid NeuGc NJ D-Neup Neuraminic acid Neu N KDN*2-Keto-3-deoxynananic acid KDN K Kdo 3-deoxy-D-manno-2 Kdo Woctulopyranosylono D-GalpA D-Galactoronic acid GalA L D-Idop D-Iodoronicacid Ido I L-Rhap L-Rhamnopyranose Rha H L-Fucp L-Fucopyranose Fuc FD-Xylp D-Xylopyranose Xyl X D-Ribp D-Ribopyranose Rib B L-ArafL-Arabinofuranose Ara R D-GlcpA D-Glucoronic acid GlcA U D-AllpD-Allopyranose All O D-Apip D-Apiopyranose Api P D-Tagp D-TagopyranoseTag T D-Abep D-Abequopyranose Abe Q D-Xulp D-Xylulopyranose Xul D D-FrufD-Fructofuranose Fru E*Another name for KDN is: 3-deoxy-D-glycero-K-galacto-nonulosonic acid.

The sugar units or other saccharide structures present in the glycans ofthe invention can be chemically modified in a variety of ways. A listingof some of the types of modifications and substituents that the sugarunits in the glycans of the invention can possess, along with theabbreviations for these modifications/substituents is provided below inTable 2. TABLE 2 Modification type Symbol Modification type Symbol AcidA Acid A N-Methylcarbamoyl ECO deacetylated N-Acetyl Q (amine) pentyl EEDeoxy Y octyl EH Ethyl ET ethyl ET Hydroxyl OH inositol IN Inositol INN-Glycolyl J Methyl ME methyl ME N-Acetyl N N-Acetyl N N-Glycolyl Jhydroxyl OH N-Methylcarbamoyl ECO phosphate P N-Sulfate QSphosphocholine PC O-Acetyl T Phosphoethanolamine (2- PE Octyl EHaminoethylphosphate) Pyrovat acetal PYR* Pentyl EE Deacetylated N-AcetylQ Phosphate P (amine) N-Sulfate QS Phosphocholine PC sulfate S or SuPhosphoethanolamine (2- PE aminoethylphosphate) O-Acetyl T Pyrovatacetal PYR* deoxy Y*when 3 is present, it means 3,4, when 4 is present it means 4,6.Bonds between sugar units are alpha (α) or beta (β) linkages, meaningthat relative to the plane of the sugar ring, an alpha bond goes downwhereas a beta bond goes up. In the shorthand notation sometimes usedherein, the letter “a” is used to designate an alpha bond and the letter“b” is used to designate a beta bond.Glycans

The invention provides compositions, libraries and arrays of glycansthat are useful for analysis of glycan binding reactions, epitopeidentification, detecting, treating and preventing disease, as well asantibody preparation. These glycans include numerous different types ofcarbohydrates and oligosaccharides. In general, the major structuralattributes and composition of the separate glycans have been identified.In some embodiments, the libraries, compositions and glycan arraysconsist of separate, substantially pure pools of glycans, carbohydratesand/or oligosaccharides. In other embodiments, glycans are used whosesource is defined but whose structures may not be known with certainty.In many embodiments, the glycans used in the invention are pure orsubstantially pure. However, some of the glycans may be a mixture ofsimilarly structured glycans, or be a mixture of glycans from the samesource. The glycans of the libraries described herein can be used tomake the glycan arrays of the invention.

The glycans of the invention include straight chain and branchedoligosaccharides as well as naturally occurring and synthetic glycans.For example, the glycan can be a glycoaminoacid, a glycopeptide, aglycolipid, a glycoaminoglycan (GAG), a glycoprotein, a whole cell, acellular component, a glycoconjugate, a glycomimetic, aglycophospholipid anchor (GPI), glycosyl phosphatidylinositol(GPI)-linked glycoconjugates, bacterial lipopolysaccharides andendotoxins. The glycans can also include N-glycans, O-glycans,glycolipids and glycoproteins.

The glycans of the invention include 2 or more sugar units. Any type ofsugar unit can be present in the glycans of the invention, including,for example, allose, altrose, arabinose, glucose, galactose, gulose,fucose, fructose, idose, lyxose, mannose, ribose, talose, xylose, orother sugar units. The tables provided herein list other examples ofsugar units that can be used in the glycans of the invention. Such sugarunits can have a variety of modifications and substituents. Someexamples of the types of modifications and substituents contemplated areprovided in the tables herein. For example, sugar units can have avariety of substituents in place of the hydrogen (H), hydroxy (—OH),carboxylate (—COO⁻), and methylenehydroxy (—CH₂—OH) substituents. Thus,lower alkyl moieties can replace any of the hydrogen atoms from thehydroxy (—OH), carboxylic acid (—COOH) and methylenehydroxy (—CH₂—OH)substituents of the sugar units in the glycans of the invention. Forexample, amino acetyl (—NH—CO—CH₃) can replace any of the hydrogen atomsfrom the hydroxy (—OH), carboxylic acid (—COOH) and methylenehydroxy(—CH₂—OH) substituents of the sugar units in the glycans of theinvention. N-acetylneuraminic acid can replace any of the hydrogen atomsfrom the hydroxy (—OH), carboxylic acid (—COOH) and methylenehydroxy(—CH₂—OH) substituents of the sugar units in the glycans of theinvention. Sialic acid can replace any of the hydrogen atoms from thehydroxy (—OH), carboxylic acid (—COOH) and methylenehydroxy (—CH₂—OH)substituents of the sugar units in the glycans of the invention. Aminoor lower alkyl amino groups can replace any of the OH groups on thehydroxy (—OH), carboxylic acid (—COOH) and methylenehydroxy (—CH₂—OH)substituents of the sugar units in the glycans of the invention. Sulfate(—SO₄ ⁻) or phosphate (—PO₄ ⁻) can replace any of the OH groups on thehydroxy (—OH), carboxylic acid (—COOH) and methylenehydroxy (—CH₂—OH)substituents of the sugar units in the glycans of the invention. Hence,substituents that can be present instead of, or in addition to, thesubstituents typically present on the sugar units include N-acetyl,N-acetylneuraminic acid, oxy (═O), sialic acid, sulfate (—SO₄ ⁻),phosphate (—PO₄ ⁻), lower alkoxy, lower alkanoyloxy, lower acyl, and/orlower alkanoylaminoalkyl.

The following definitions are used, unless otherwise described: Alkyl,alkoxy, alkenyl, alkynyl, etc. denote both straight and branched groups;but reference to an individual radical such as propyl embraces only thestraight chain radical, when a branched chain isomer such as isopropylhas been specifically referred to. Halo is fluoro, chloro, bromo, oriodo.

Specifically, lower alkyl refers to (C₁-C₆)alkyl, which can be methyl,ethyl, propyl, isopropyl, butyl, iso-butyl, sec-butyl, pentyl, 3-pentyl,or hexyl; (C₃-C₆)cycloalkyl can be cyclopropyl, cyclobutyl, cyclopentyl,or cyclohexyl; (C₃-C₆)cycloalkyl(C₁-C₆)alkyl can be cyclopropylmethyl,cyclobutylmethyl, cyclopentylmethyl, cyclohexylmethyl,2-cyclopropylethyl, 2-cyclobutylethyl, 2-cyclopentylethyl, or2-cyclohexylethyl; (C₁-C₆)alkoxy can be methoxy, ethoxy, propoxy,isopropoxy, butoxy, iso-butoxy, sec-butoxy, pentoxy, 3-pentoxy, orhexyloxy.

It will be appreciated by those skilled in the art that the glycans ofthe invention having one or more chiral centers may exist in and beisolated in optically active and racemic forms. Some compounds mayexhibit polymorphism. It is to be understood that the present inventionencompasses any racemic, optically-active, polymorphic, orstereoisomeric form, or mixtures thereof, of a glycan of the invention.Procedures available in the art can be used to prepare optically activeforms (for example, by resolution of the racemic form byrecrystallization techniques, by synthesis from optically-activestarting materials, by chiral synthesis, or by chromatographicseparation using a chiral stationary phase).

Specific and preferred values listed below for substituents and ranges,are for illustration only; they do not exclude other defined values orother values within defined ranges or for the substituents.

The libraries, arrays and compositions of the invention are particularlyuseful because diverse glycan structures are difficult to make andsubstantially pure solutions of a single glycan type are hard togenerate. For example, because the sugar units typically present inglycans have several hydroxyl (—OH) groups and each of those hydroxylgroups is substantially of equal chemical reactivity, manipulation of asingle selected hydroxyl group is difficult. Blocking one hydroxyl groupand leaving one free is not trivial and requires a carefully designedseries of reactions to obtain the desired regioselectivity andstereoselectivity. Moreover, the number of manipulations requiredincreases with the size of the oligosaccharide. Hence, while synthesisof a disaccharide may require 5 to 12 steps, as many as 40 chemicalsteps can be involved in synthesis of a typical tetrasaccharide. In thepast, chemical synthesis of oligosaccharides was therefore fraught withpurification problems, low yields and high costs. However the inventionhas solved these problems by providing libraries and arrays of numerousstructurally distinct glycans.

The glycans of the invention have been obtained by a variety ofprocedures. For example, some of the chemical approaches developed toprepare N-acetyllactosamines by glycosylation between derivatives ofgalactose and N-acetylglucosamine are described in Aly, M. R. E.;Ibrahim, E. -S. I.; El-Ashry, E. -S. H. E. and Schmidt, R. R.,Carbohydr. Res. 1999, 316, 121-132; Ding, Y.; Fukuda, M. and Hindsgaul,O., Bioorg. Med. Chem. Lett. 1998, 8, 1903-1908; Kretzschmar, G. andStahl, W., Tetrahedr. 1998, 54, 6341-6358. These procedures can be usedto make the glycans of the present invention, but because there aremultiple tedious protection/deprotection steps involved in such chemicalsyntheses, the amounts of products obtained in these methods can be low,for example, in milligram quantities.

One way to avoid protection-deprotection steps typically required duringglycan synthesis is to mimic nature's way of synthesizingoligosaccharides by using regiospecific and stereospecific enzymes,called glycosyltransferases, for coupling reactions between themonosaccharides. These enzymes catalyze the transfer of a monosaccharidefrom a glycosyl donor (usually a sugar nucleotide) to a glycosylacceptor with high efficiency. Most enzymes operate at room temperaturein aqueous solutions (pH 6-8), which makes it possible to combineseveral enzymes in one pot for multi-step reactions. The highregioselectivity, stereoselectivity and catalytic efficiency makeenzymes especially useful for practical synthesis of oligosaccharidesand glycoconjugates. See Koeller, K. M. and Wong, C.-H., Nature 2001,409, 232-240; Wymer, N. and Toone, E. J., Curr. Opin. Chem. Biol. 2000,4, 110-119; Gijsen, H. J. M.; Qiao, L.; Fitz, W. and Wong, C.-H., Chem.Rev. 1996, 96, 443-473.

Recent advances in isolating and cloning glycosyltransferases frommammalian and non-mammalian sources such as bacteria facilitateproduction of various oligosaccharides. DeAngelis, P. L., Glycobiol.2002, 12, 9R-16R; Endo, T. and Koizumi, S., Curr. Opin. Struct. Biol.2000, 10, 536-541; Johnson, K. F., Glycoconj. J. 1999, 16, 141-146. Ingeneral, bacterial glycosyltransferases are more relaxed regarding donorand acceptor specificities than mammalian glycosyltransferases.Moreover, bacterial enzymes are well expressed in bacterial expressionsystems such as E. coli that can easily be scaled up for over expressionof the enzymes. Bacterial expression systems lack the post-translationalmodification machinery that is required for correct folding and activityof the mammalian enzymes whereas the enzymes from the bacterial sourcesare compatible with this system. Thus, in many embodiments, bacterialenzymes are used as synthetic tools for generating glycans, rather thanenzymes from the mammalian sources.

For example, the repeating Galβ(1-4)GlcNAc-unit can be enzymaticallysynthesized by the concerted action of β4-galactosyltransferase (β4GalT)and β3-N-acetyllactosamninyltransferase (β3GlcNAcT). Fukuda, M.,Biochim. Biophys. Acta. 1984, 780:2, 119-150; Van den Eijnden, D. H.;Koenderman, A. H. L. and Schiphorst, W. E. C. M., J. Biol. Chem. 1988,263, 12461-12471. The inventors have previously cloned and characterizedthe bacterial N. meningitides enzymes β4GalT-GalE and β3GlcNAcT anddemonstrated their utility in preparative synthesis of variousgalactosides. Blixt, O.; Brown, J.; Schur, M.; Wakarchuk, W. andPaulson, J. C., J. Org. Chem. 2001, 66, 2442-2448; Blixt, O.; van Die,I.; Norberg, T. and van den Eijnden, D. H., Glycobiol. 1999, 9,1061-1071. β4GalT-GalE is a fusion protein constructed from β4GalT andthe uridine-5′-diphospho-galactose-4′-epimerase (GalE) for in situconversion of inexpensive UDP-glucose to UDP-galactose providing a costefficient strategy. Further examples of procedures used to generate theglycans, libraries and arrays of the invention are provided in theExamples.

In most cases, the structures of the glycans used in the compositions,libraries and arrays of the invention are described herein. However, insome cases a source of the glycan, rather than the precise structure ofthe glycan is given. Hence, a glycan from any available natural sourcecan be used in the arrays and libraries of the invention. For example,known glycoproteins are a useful source of glycans. The glycans fromsuch glycoproteins can be isolated using available procedures or, forexample, procedures provided herein. Such glycan preparations can thenbe used in the compositions, libraries and arrays of the invention.

Examples of glycans provided in the libraries and on the arrays of theinvention are provided in Table 3. Glycans 1-200 in Table 3 correspondto glycans 1-200 shown in FIG. 7. TABLE 3 1 AGP (acid glycoprotein)mixture of bi and tri- and tetra-antenary N- glyclans 2 AGP-A (acidglycoprotein A) mixture of bi and tri-antenary N-glycans 3 AGP-B (acidglycoprotein B) mixture of bi and tri-antenary N-glycans 4Ceruloplasmine mixture of bi and tri- and tetra-antenary N-glycans 5Fibrinogen mixture of biantenary-N-glycans 6 Transferrin mixture of biand tri- and tetra-antenary N-glycans 7Galβ1-4(Fuc1-3)GlcNAcβ1-4Galβ1-4(Fuc1-3)GlcNAcβSp 8Galβ1-4(Fucα1-3)GlcNAcβ1-4Galβ1-4(Fucα1-3)GlcNAcβ1-4Galβ1-4(Fucα1-3)GlcNAcfβSp 9Galfβ1-4GlcNAcβ1-4Galβ1-4GlcNAcβ1-4Galβ1-4GlcNAcβSp 10 Gal[3S]βSp 11Gal[3S]β1-3GalNAcαSp 12 Gal[3S]β1-3GlcNAcβSp 13 Gal[3S]β1-4Glc[6S]βSp 14Gal[3S]β1-4Glc[6S]βSp 15 Gal[3S]β1-4GlcβSp 16 Gal[3S]β1-4GlcNAcβSp 17Gal[4S]β1-4GlcNAcβSp 18 Man[6P]αSp 19 Gal[6S]β1-4Glc[6S]βSp 20Gal[6S]β1-4GlcβSp 21 Gal[6S]β1-4GlcβSp 22 GlcNAc[6S]βSp 23(GlcNAcβ1-3(GlcNAcβ1-6)GlcNAcβ1-4)GalNAcaSp 24NeuAcα2-3Galβ1-3(NeuAcα2-3Galβ1-4)GlcNAcβSp 25Gal[3S]β1-3(Fucα1-4)GlcNAcβSp 26 Gal[3S]β1-4(Fucα1-3)GlcNAcβSp 279[NAc]NeuAcαSp 28 9[NAc]NeuAcα2-6Galβ1-4GlcNAcβSp 29 GalαSp 30Galα1-2Galβ-Sp 31 Galα1-3(Galα1-4)Galβ1-4GlcNAcβSp 32Galα1-3(Fucα1-2)Galβ-Sp 33 Galα1-3GalβSp 34Galα1-3Galβ1-4(Fucα1-3)GlcNAcβSp 35 Galα1-3Galβ1-4GlcβSp 36Galα1-3(Fucα1-2)Galβ1-4GlcNAcβSp 37 Galα1-3Galβ1-4GlcNAcβSp 38Galα1-3GalNAcαSp 39 Galα1-3GalNAcβSp 40 Galα1-4(Fucα1-2)Galβ1-4GlcNAcβSp41 Galα1-4Galβ1-4GlcβSp 42 Galα1-4Galβ1-4GlcNAcβSp 43Galα1-4Galβ1-4GlcNAcβSp 44 Galα1-4GlcNAcβSp 45 Galα1-6GlcβSp 46 GalβSp47 Galβ1-3(NeuAcα2-6)GalNAcαSp 48 Galβ1-2GalβSp 49Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcαSp 50 Galβ1-3(Fucα1-4)GlcNAcβSp 51Galβ1-3(Fucα1-4)GlcNAcβSp 52 Galβ1-3(GlcNAcβ1-6)GalNAcαSp 53Galβ1-3(NeuAcα2-6)GlcNAcβ1-4Galβ1-4GlcβSp 54 Galβ1-3(NeuAcβ2-6)GalNAcαSp55 Galβ1-3GalβSp 56 Galβ1-3GalNAcαSp 57 Galβ1-3GlcNAcβSp 58Galβ1-3GalNAcβ1-4(NeuAcα2-3)Galβ1-4GlcβSp 59Galβ1-3GalNAcβ1-4Galβ1-4GlcβSp 60 Galβ1-3GlcNAcαSp 61 Galβ1-3GlcNAcβSp62 Galβ1-3GlcNAcβ1-3Galβ1-4GlcβSp 63 Galβ1-4Glc[6S]βSp 64Galβ1-4Glc[6S]βSp 65 Galβ1-4(Fucα1-3)GlcNAcβSp 66Galβ1-4(Fucα1-3)GlcNAcβSp 67 Galβ1-4GalNAcα1-3(Fucα1-2)Galβ1-4GlcNAcβSp68 Galβ1-4GlcβSp 69 Galβ1-4GlcβSp 70 Galβ1-4GlcNAcβSp 71Galβ1-4GlcNAcβSp 72 Galβ1-4GlcNAcβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcαSp 73Galβ1-4GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-4 (Fucα1-3)GlcNAcβSp 74Galβ1-4GlcNAcβ1-3Galβ1-4GlcβSp 75 Galβ1-4GlcNAcβ1-3Galβ1-4GlcβSp 76Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβSp 77 Galβ1-4GlcNAcβ1-3GalNAcαSp 78Galβ1-4GlcNAcβ1-3GalNAcαSp 79 Galβ1-4GlcNAcβ1-6GalNAcαSp 80 GalNAcαSp 81GalNAcα1-3(Fucα1-2)GalβSp 82 GalNAcα1-3GalββSp 83GalNAcα1-3(Fuca1-2)Galβ1-4GlcNAcβSp 84 GalNAcα1-3GalNAcβSp 85GalNAcα1-4(Fucα1-2)Galβ1-4GlcNAcβSp 86 GalNAcβSp 87GalNAcβ1-3(Fucα1-2)GalβSp 88 GalNAcβ1-3GalNAcαSp 89 GalNAcβ1-4GlcNAcβSp90 GalNAcβ1-4GlcNAcβSp 91 FucαSp 92 FucαSp 93 Fucα1-2GalβSp 94Fucα1-2Galβ1-3(Fucα1-4)GlcNAcβ-Sp 95 Fucα1-2Galβ1-3GalNAcβ-Sp 96Fucα1-2Galβ1-3GalNAcβ1-3GalαSp 97Fucα1-2Galβ1-3GalNAcβ1-3Galβ1-4Galβ1-4GlcβSp 98Fucα1-2Galβ1-3GalNAcβ1-4(NeuAcα2-3)Galβ1-4GlcβSp 99Fucα1-2Galβ1-3GlcNAcβSp 100 Fucα1-2Galβ1-3GlcNAcβSp 101Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβSp 102 Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβSp103 Fucα1-2Galβ1-4GlcβSp 104 Fucα1-2Galβ1-4GlcNAcβSp 105Fucα1-2Galβ1-4GlcNAcβSp 106 Fucα1-2Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβSp 107Fucα1-2Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβSp 108Fucα1-2GlcNAcβSp 109 Fucα1-3GlcNAcβSp 110 Fucα1-3GlcNAcβSp 111Fucα1-2Galβ1-3GalNAcβ1-4(NeuAcα1-3)Galβ1-4GlcβSp 112 GlcαSp 113Glcβ1-4GlcβSp 114 GlcβSp 115 Glcβ1-4GlcβSp 116 Glcβ1-6GlcβSp 117GlcNAcβSp 118 GlcNAcβSp 119 GlcNAcβ1-2Galβ1-3GalNAcαSp 120GlcNAcβ1-3(GlcNAcβ1-6)GalNAcαSp 121 GlcNAcβ1-3GalβSp 122GlcNAcβ1-3Galβ1-3GalNAcαSp 123 GlcNAcβ1-3Galβ1-4GlcβSp 124GlcNAcβ1-3Galβ1-4GlcNAcβSp 125 GlcNAcβ1-4(GlcNAcβ1-6)GalNAcαSp 126GlcNAcβ1-4GlcNAcβ1-4GlcNAcβSp 127 GlcNAcβ1-4Mur-L-Ala-D-GlnβSp 128GlcNAcβ1-6GalNAcαSp 129 Glc-ol-amine 130 GlcAαSp 131 GlcAβSp 132KDNα2-3Galβ1-3GlcNAcβSp 133 KDNα2-3Galβ1-4GlcNAcβSp 134 ManαSp 135Manα1-2Manα1-2Manα1-3ManαSp 136 Manα1-2Manα1-3(Manα1-2Manα1-6)ManαSp 137Manα1-2Manα1-3ManαSp 138 Manα1-3(Manα1-2Manα1-2Manα1-6)ManαSp 139Manα1-3(Manα1-6)ManαSp 140Manα1-3Manα1-6(Manα1-2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 141Man5-Man9βSp-mixture(mixture is of glycans 140, 142-145) 142Manα1-6(Manα1-3)Manα1-6(Manα1-2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 143Manα1-6(Manα1-2Manα1-3)Manα1-6(Manα1-2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 144Manα1-2Manα1-6(Manα1-3)Manα1-6(Manα1-2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 145 Manα1-2Manα1-2Manα1-3(Manα1-2Manα1-3(Manα1-2Manα1-6)Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 146 NeuAcα2-8NeuAcαSp 147NeuAcα2-8NeuAcα2-8NeuAcαSp 148 NeuGcαSp 149NeuGcα2-3Galβ1-3(Fucα1-4)GlcNAcβSp 150 NeuGcα2-3Galβ1-3GlcNAcβSp 151NeuGcα2-3Galβ1-4(Fucα1-3)GlcNAcβSp 152 NeuGcα2-3Galβ1-4GlcβSp 153NeuGcα2-3Galβ1-4GlcNAcβSp 154 NeuGcα2-6Galβ1-4GlcNAcαSp 155NeuGcα2-6GalNAcαSp 156 NeuAcαSp 157 NeuAcα2-3(6S)Galβ1-4GlcNAcβSp 158NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcβSp 159NeuAcα2-3(Galβ1-3GalNAcβ1-4)Galβ1-4GlcNAcβSp 160NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcNAcβSp 161NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-4Galβ1-4(Fucα1-3)GlcNAcβ1-4Galβ1-4(Fucα1-3)GlcNAcβSp 162 NeuAcα2-3GalβSp 163NeuAcα2-3Galβ1-3GalNAc[6S]αSp 164 NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcβSp 165NeuAcα2-3Galβ1-3(NeuAcα2-6)GalNAcαSp 166 NeuAcα2-3Galβ1-3GalNAcαSp 167NeuAcα2-3Galβ1-4GlcNAc[6S]βSp 168 NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc[6S]βSp169 NeuAcα2-3Galβ1-4GlcNAc[6S]βSp 170NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc[6S]βSp 171NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβSp 172NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβSp 173NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-3GalβSp 174NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-4GlcNAcβSp 175NeuAcα2-3Galβ1-4GlcβSp 176 NeuAcα2-3Galβ1-4GlcβSp 177NeuAcα2-3Galβ1-4GlcNAcβSp 178 NeuAcα2-3Galβ1-4GlcNAcβSp 179NeuAcα2-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβSp 180NeuAcα2-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβ1-3Galβ1- 4GlcNAcβSp 181NeuAcα2-6GalNAcαSp 182 NeuAcα2-6GalβSp 183 NeuAcα2-6Galβ1-4GlcNAc[6S]βSp184 NeuAcα2-6Galβ1-4GlcβSp 185 NeuAcα2-6Galβ1-4GlcβSp 186NeuGcα2-6Galβ1-4GlcNAcαSp 187 NeuGcα2-6Galβ1-4GlcNAcαSp 188NeuAcα2-6Galβ1-4GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβSp 189 NeuAcα2-6Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβSp 190NeuAcβ2-6GalNAcαSp 191 NeuAcα2-8NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcβSp 192NeuAcα2-8NeuAcα2-3Galβ1-4GlcβSp 193NeuAcα2-8NeuAcα2-8NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcβSp 194NeuAcα2-8NeuAcα8NeuAcα2-3Galβ1-4GlcβSp 195 NeuAcα2-3(NeuAcα2-6)GalNAcαSp196 NeuAcβSp 197 NeuAcβ2-6Galβ1-4GlcNAcβSp 198 NeuAcβ2-6GalNAcαSp 199NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-3(NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 200 RhaαSp 201 ManβSp 202±(NeuAcα2-6)Galβ1-4GlcNAcα1-2Manα1-6(±(NeuAcα2-6)Galβ1-4GlcNAcα1-2Manα1-3)Manβ1-4 GlcNAcβ1-4GlcNAcβSp 203 GalNAc[3S]βSp 204 GalNAc[6S]βSp205 Galβ1-4GlcNAcβ1-2Manα1-3(Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 206 Fucα1-2Galβ1-3GlcNAcβ1-3Galβ1-4GlcβSp 207Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβ1-4Galβ1-4(Fucα1-3)GlcNAcβSp 208Fucα1-4GlcNAcβSp 209 Galα1-3(Fucα1-2)Galβ1-4GlcβSp 210GalNAcα1-3(Fucα1-2)Galβ1-4GlcβSp 211GalNAcβ1-4(Fucα1-2)GlcNAcβ1-4Manα1-3(GalNAcβ1-4(Fucα1-2)GlcNAcβ1-4Manα1-6)Manβ1-4 GlcNAcβ1-4(Fucα1-2)GlcNAcβSp 212GalNAcβ1-4(Fucα1-3)GlcNAcβSp 213GalNAcβ1-4GlcNAcβ1-4Manα1-6(GalNAcβ1-4GlcNAcβ1-4Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 214 Galα1-4(Fucα1-2)Galβ1-4GlcNAcβSp 215Galβ1-3(Galβ1-3Galβ1-4GlcNAcβ1-6)GalNAcαSp 216Galβ1-3(Galβ1-4(Fucα1-3)GlcNAcβ1-6)GalNAcαSp 217Galβ1-3(NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-6)GalNAcαSp 218Galβ1-3(NeuAcα2-3Galβ1-4GlcNAcβ1-6)GalNAcαSp 219 Galβ1-4GlcNAc[6S]βSp220 Galβ1-4(Fucα1-3)GlcNAcβ1-4Manα1-6(Galβ1-4(Fucα1-3)GlcNAcβ1-4Manα1-6)Manβ1-4GlcNAcβ1-4 GlcNAcβSp 221Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβSp 222Galβ1-4GlcNAcβ1-4Manα1-3(Galβ1-4GlcNAcβ1-4Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 223 Galβ1-4GlcNAcβ1-6(Galβ1-3)GalNAcαSp 224GlcNAcβ1-2Manα1-3(GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1- 4(Fucα1-6)GlcNAcβSp225 GlcNAcβ1-3GalNAcαSp 226 GlcNAcβ1-4GlcNAcβ1-4GlcNAcβ1-4GlcNAcβSp 227GlcNAcβ1-4GlcNAcβSp 228 GlcNAcβ1-4GlcNAcβSp 229GlcNAcβ1-6(Galβ1-3)GalNAcαSp 230Manα1-2Manα1-3(Mancα1-6)Manβ1-4GlcNAcβ1-4(Fucα1- 3)GlcNAβSp 231Manα1-3(Xylβ1-2)(Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 232Manα1-2Manα1-6(Manα1-3)Manα1-6(Manα2Manα2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 233 Manα1-3(Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 234Manα1-6(Manα1-3)Manα1-6(GlcNAcβ1-4)(GlcNAcβ1-2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 235Manα1-6(Manα1-3)Manβ1-4GlcNAcβ1-4(Fucα1-2)GlcNAcβSp 236Manα1-6(Manα1-3)Manα1-6(Manα1-3)Manβ1-4GlcNAcβ1-4 GlcNAcβSp 237Manα1-6Manα1-3(Manα1-6Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAcβSp 238 mixedbiantennary glycansβSp 239 mixed N-glycansβSp 240NeuAcα2-3(Galβ1-3GlcNAcβ1-4)Galβ1-4GlcβSp 241NeuAcα2-3Galβ1-3(Galβ1-3Galβ1-4GlcNAcβ1-6)GalNAcαSp 242NeuAcα2-3Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcαSp 243NeuAcα2-3Galβ1-3(GlcNAcβ1-6)GalNAcαSp 244NeuAcα2-3Gal[6S]β1-4(Fucα1-3)GlcNAcβSp 245NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcβSp 246 NeuAcα2-3GalNAcαSp 247NeuAcα2-3Galβ1-3(Galβ1-4(Fucα1-3)GlcNAcβ1-6)GalNAcαSp 248NeuAcα2-3Galβ1-3(NeuAcα2-3Galβ1-4)GlcNAcβSp 249NeuAcα2-3Galβ1-3(NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1- 6)GalNAcαSp 250NeuAcα2-3Galβ1-3(NeuAcα2-3Galβ1-4GlcNAcβ1-6)GalNAcαSp 251NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβSp 252NeuAcα2-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβSp 253 NeuAcα2-3Galβ1-4GlcNAcβSp254 NeuAcα2-6(Galβ1-3)GalNAcαSp 255NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-6((NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4 GlcNAcβSp 256NeuAcα2-6Galβ1-4GlcNAcβ1-4Galβ1-4GlcNAcβSp 257NeuAcα2-8NeuAcα2-3Galβ1-4GlcβSp 258 NeuAcα2-8NeuAcα2-8NeuAcαSp 259NeuAcβ2-6(Galβ1-3)GalNAcβSp 260 NeuGcα2-3Galβ1-3(Fucα1-4)GlcNAcβSp 261NeuGcα2-3Galβ1-3GlcNAcβSp 262 NeuGcα2-3Galβ1-4(Fucα1-3)GlcNAcβSp 263NeuGcβSp 264 NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-3(Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4(Fucα1-6) GlcNAcβSp 265NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-3(NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4 (Fuc1α1-6)GlcNAcβSp 266NeuAcα2-8NeuAcα2-(3-6)Galβ1-4GlcNAcβ1-2Manα1-3(NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4(Fucα1-6) GlcNAcβSp 267NeuAcα2-8NeuAcα2-8NeuAcα2-(3-6)Galβ1-4GlcNAcβ1-2Manα1-3(NeuAcα2-6Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1- 4(Fucα1-6)GlcNAcβSp269 GlcNAcβ1-3(GlcNAcβ1-4)Galβ1-4GlcNAcβSp 270GlcNAcβ1-3Galβ1-4GlcNAcβSp 271 GlcAβ1-3GalβSp 272GlcNAcβ1-4GlcNAcβ1-4GlcNAcβ1-4GlcANAcβ1-4GlcNAcβSp 273GlcNAcβ1-6Galβ1-4GlcNAcβSp 274 Glcα1-4Glc1-4αSp 275 Glcα1-6Glc,6αGlcαSp276 GlcNAcβ1-4Galβ1-4GlcNAcβSp 277 Galβ1-4GlcNAc[6S]βSp 278GlcNAcβ1-4GlcNAcβ1-4GlcNAcβ1-4GlcNAcβ1-4GlcANAcβ1- 4GlcNAcβSp 279GlcNGcβSp 280 Manβ1-4GlcNAcβSp 281 Gal[6S]β1-4GlcNAcβSp 282Galβ1-4GlcNAcβ1-2Manα1-3(Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 283GlcNAcβ1-2Manα1-3(GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1- 4GlcNAcβSp 284Manα1,3(Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβSp 285Galα1-3(Fucα1-2)Galβ1-3GlcNAcβSp 286 GalNAcα1-3(Fucα1-2)Galβ1-3GlcNAcβSp287 GalNAcα1-3(Fucα1-2)Galβ1-4(Fucα1-3)GlcNAcβSp 288Galα1-3(Fucα1-2)Galβ1-4(Fucα1-3)GlcNAcβSp 289Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβSp 290 GalNAcα1-3(Fucα1-2)Galβ1-4GlcβSp 291Galα1-3(Fucα1-2)Galβ1-4GlcβSp 292NeuAcα2-3Galβ1-3GlcNAcβ1-3Galβ1-4GlcNAcβSp 293NeuAcα2-6Galβ1-3GlcNAcβ1-3Galβ1-4GlcNAcβSp 294GalNAcβ1-4(Fucα1-3)GlcNAcβSp 295 Galβ1-3GlcNAcβ1-3Galβ1-4GlcβSp 296GalNAcβ1-3Galα1-4Galβ1-4GlcβSp 297 Galβ1-3GalNAcβ1-3Galα1-4Galβ1-4GlcβSp298 NeuAcα2-3Galβ1-3GalNAcβ1-3Galα1-4Galβ1-4GlcβSp 299Fucα1-2Galβ1-3GalNAcβ1-3Galα1-4Galβ1-4GlcβSp 300Fucα1-2Galβ1-3(Fucα1-4)GlcNAcβ1-3Galβ1-4(Fucα1-3)GlcNAcβSp 301NeuAcα2-3Galβ1-3(Fucα1-4)GlcNAcβ1-3Galβ1-4GlcNAcβSp 302NeuAcα2-3Galβ1-3(Fucα1-4)GlcNAcβ1-3Galβ1-4(Fucα1- 3)GlcNAcβSp 203NeuAcα2-8NeuAcα2-3(Galβ1-3GalNAcβ1-4)Galβ1-4GlcβSp 304NeuAcα2-8NeuAcα2-3(NeuAcα2-3Galβ1-3GalNAcβ1-4)Galβ1- 4GlcβSp 305NeuAcα2-3(Galβ1-3GalNAcβ1-4)Galβ1-4GlcβSp 306NeuAcα2-3(NeuAcα2-3Galβ1-3GalNAcβ1-4)Galβ1-4GlcβSp 307NeuAcα2-8NeuAcα2-8-NeuAcα2-3(Galβ1-3GalNAcβ1-4)Galβ1- 4GlcβSp 308NeuAcα2-8NeuAcα2-8-NeuAcα2-3(NeuAcα2-3Galβ1-3GalNAcβ1- 4)Galβ1-4GlcβSp309 NeuAcα2-8NeuAcα2-8NeuAcα2-8-NeuAcα2-3(Galβ1-3GalNAcβ1-4)Galβ1-4GlcβSp 310 NeuAcα2-8NeuAcα2-8NeuAcα2-8NeuAcα1-3(NeuAcα2-3Galβ1-3GalNAcβ1-4)Galβ1-4GlcβSp 311NeuAcα2-8NeuAcα2-8NeuAcα2-8-NeuAcα2-3(GalNAcβ1-4)Galβ1- 4GlcβSp 312Galβ1-4GlcNAcβ1-2(Galβ1-4GlcNAcβ1-4)Manα1-3[Galβ1-4GlcNAcβ1-3(Galβ1-4GlcNAcβ1-6)Manα1-6]Manβ1-4GlcNAcβ1-4GlcNAcβSpMany of the abbreviations employed in the table are defined herein or atthe website functionalglycomics.org. In particular, the followingabbreviations were used: Sp means “spacer.”

The glycans of the invention can have spacers, linkers, labels, linkingmoieties and/or other moieties attached to them. These spacers, linkers,labels, linking moieties and/or other moieties can be used to attach theglycans to a solid support, detect particular glycans in an assay,purify or otherwise manipulate the glycans. For example, the glycans ofthe invention can have amino moieties provided by attached alkylaminegroups, amino acids, peptides, or proteins. In some embodiments, theglycans have alkylamine moieties such as —OCH₂CH₂NH₂ (called Sp1), or—OCH₂CH₂CH₂NH₂ (called Sp2 or Sp3), or NH—(CO)(CH₂)₂—NH—(called Sp4), orCH₂)₄—NH (called Sp5) that have useful as linking moieties (the amine)and act as spacers or linkers.

Glycan Arrays

The arrays of the invention employ a library of characterized anddefined glycan structures. The array has been validated with a diverseset of carbohydrate binding proteins such as plant lectins and C-typelectins, Siglecs, Galectins, Influenza Hemagglutinins andanti-carbohydrate antibodies (from crude sera, purified serum fractionsand purified monoclonal antibody preparations).

The inventive libraries, arrays and methods have several advantages. Oneparticular advantage of the invention is that the arrays and methods ofthe invention provide highly reproducible results.

Another advantage is that the libraries and arrays of the inventionpermit screening of multiple glycans in one reaction. Thus, thelibraries and arrays of the invention provide large numbers andvarieties of glycans. For example, the libraries and arrays of theinvention have at least two glycans, at least three glycans, at leastten glycans, at least 30 glycans, at least 40 glycans, at least 50glycans, at least 100 glycans, at least 150 glycans, at least 175glycans, at least 200 glycans, at least 250 glycans or at least 500glycans. In some embodiments, the libraries and arrays of the inventionhave more than two glycans, more than three glycans, more than tenglycans, more than 40 glycans, more than 50 glycans, more than 100glycans, more than 150 glycans, more than 175 glycans, more than 200glycans, more than 250 glycans or more than 500 glycans. In otherembodiments, the libraries and arrays of the invention have about 2 toabout 100,000, or about 2 to about 10,000, or about 2 to about 7500, orabout 2 to about 1,000, or about 2 to about 500, or about 2 to about200, or about 2 to 100 different glycans per library or array. In otherembodiments, the libraries and arrays of the invention have about 50 toabout 100,000, or about 50 to about 10,000, or about 50 to about 7500,or about 50 to about 1,000, or about 50 to about 500, or about 50 toabout 200 different glycans per library or array. Such large numbers ofglycans permit simultaneous assay of a multitude of glycan types.

Moreover, as described herein, the present arrays have been used forsuccessfully screening a variety of glycan binding proteins. The glycanarrays of the invention are reusable after stripping with acidic, basicaqueous or organic washing steps. Experiments demonstrate that littledegradation of the glyean occurs and only small amounts of glycanbinding proteins are consumed during a screening assay. Hence, thearrays of the invention can be used for more than one assay.

The arrays and methods of the invention provide high signal to noiseratios. The screening methods provided by the invention are fast andeasy because they involve only one or a few steps. No surfacemodifications or blocking procedures are typically required during theassay procedures of the invention.

The composition of glycans on the arrays of the invention can be variedas needed by one of skill in the art. Many different glycoconjugates canbe incorporated into the arrays of the invention including, for example,purified glycans, naturally occurring or synthetic glycans,glycoproteins, glycopeptides, glycolipids, bacterial and plant cell wallglycans and the like. Immobilization procedures for attaching differentglycans to the arrays of the invention are readily controlled to easilypermit array construction.

Spacer molecules or groups can be used to link the glycans to thearrays. Such spacer molecules or groups include fairly stable (e.g.substantially chemically inert) chains or polymers. For example, thespacer molecules or groups can be alkylene groups. One example of analkylene group is —(CH₂)n-, where n is an integer of from 1 to 20. Insome embodiments, n is an integer of from 1 to 10.

Unique libraries of different glycans are attached to defined regions onthe solid support of the array surface by any available procedure. Ingeneral, the arrays are made by obtaining a library of glycan molecules,attaching spacer molecules with linking moieties to the glycans in thelibrary, obtaining a solid support that has a surface derivatized toreact with the specific linking moieties present on the glycans of thelibrary and attaching the glycan molecules to the solid support byforming a covalent linkage between the linking moieties and thederivatized surface of the solid support.

The derivatization reagent can be attached to the solid substrate viacarbon-carbon bonds using, or example, substrates having(poly)trifluorochloroethylene surfaces, or more preferably, by siloxanebonds (using, for example, glass or silicon oxide as the solidsubstrate). Siloxane bonds with the surface of the substrate are formedin one embodiment via reactions of derivatization reagents bearingtrichlorosilyl or trialkoxysilyl groups.

For example, a glycan library can be employed that has been modified tocontain primary amino groups. Thus, in some embodiments, the glycans ofthe invention can have amino moieties provided by attached alkylaminegroups, amino acids, peptides, or proteins. For example, the glycans canhave alkylamine groups such as the —OCH₂CH₂NH₂ (called Sp1) or—OCH₂CH₂CH₂NH₂ (called Sp2 or Sp3), or NH—(CO)(CH₂)₂—NH— (called Sp4),or CH₂)₄—NH (called Sp5) groups attached that provide the primary aminogroup. The primary amino groups on the glycans can react with anN-hydroxy succinimide (NHS)-derivatized surface of the solid support.Such NHS-derivatized solid supports are commercially available. Forexample, NHS-activated glass slides are available from Accelr8Technology Corporation, Denver, Colo. (now Schott Nexterion, Germany).After attachment of all the desired glycans, slides can further beincubated with ethanolamine buffer to deactivate remaining NHSfunctional groups on the solid support. The array can be used withoutany further modification of the surface. No blocking procedures toprevent unspecific binding are typically needed. FIG. 1 provides aschematic diagram of such a method for making arrays of glycanmolecules.

Each type of glycan is contacted or printed onto to the solid support ata defined glycan probe location. Suitable printing methods include piezoor pin printing techniques. A microarray gene printer can be used forapplying the various glycans to defined glycan probe locations. Theprinting process is shown diagrammatically in FIG. 1. Printing in the Xdirection gives rise “columns” of glycans and printing in the directionorthogonal to the X direction gives rise to “rows.” During printing, theinkjet is generally stationary, and a stepping stage moves the glassslide or other solid surface over the head in the X direction. As thewafer passes over the head, it prints the appropriate glycan to eachglycan probe location. Several nozzles simultaneously dispense aselected amount of glycan solution.

For example, about 0.1 nL to about 10 nL, or about 0.5 nL of glycansolution can be applied per defined glycan probe location. Variousconcentrations of the glycan solutions can be contacted or printed ontothe solid support. For example, a glycan solution of about 0.1 to about1000 μM glycan or about 1.0 to about 500 μM glycan or about 10 to about100 μM glycan can be employed. In general, it may be advisable to applyeach concentration to a replicate of several (for example, three to six)defined glycan probe locations. Such replicates provide internalcontrols that confirm whether or not a binding reaction between a glycanand a test molecule is an actual binding interaction.

Methods of Detecting Glycan Binding

It is contemplated that the arrays of this invention will be useful forscreening chemical and molecular biological libraries for newtherapeutic agents, for identifying ligands for known biologicalreceptors and new receptors for known ligands, for identifying epitopes,characterizing antibodies, genotyping human populations for diagnosticand therapeutic purposes, and many other uses. Any such ligands,receptors, lectins galectins, antibodies, proteins and like can bepotential glycan binding entities that can be detected using the arraysand methods provided herein.

The arrays of the invention are intended for use in a molecularrecognition-based assay, in which a sample that may contain a glycanbinding entity is brought into contact with an array of glycans of knownsource or structure, that are located at predetermined spatial positions(glycan probe locations) on the support surface of the array. Binding isrecognized by detection of a label at a specific glycan probe locationon the array, where the label is directly or indirectly associated witha glycan binding entity. Binding of a glycan binding entity is ofsufficiently high affinity to permit the entity to be retained by theglycan array during washing and until detection of the associated labelhas been accomplished.

In using an array of the invention, the identity of a lectin, antibody,protein, molecule, or chemical moiety bound to a glycan at anyparticular location in the array can be determined by detecting thelocation of the label associated with the bound entity and linking thiswith the array's tagged file. The tagged file is a file of informationwherein the identity and position of each glycan in the array pertainingto the file is stored. There are various methods of linking this taggedfile with the physical array. For example, the tagged file can bephysically encoded on the array or its housing by means of a siliconchip, magnetic strip or bar code. Alternatively, the informationidentifying the array to a particular tagged file might be included onan array or its housing, with the actual file stored in the dataanalysis device or in a computer in communication with the device. Thelinking of the tagged file with the physical array would take place atthe time of data analysis. Yet another way of doing this would be tostore the tagged file in a device such as a disc or card that could beinserted into the data analysis device by the array user at the time thearray was used in the assay.

The label can be directly associated with the glycan binding entity, forexample, by covalent linkage between the label and a purified glycanbinding entity. Alternatively, the label can be indirectly associatedwith the glycan binding entity. For example, the label can be covalentlyattached to a secondary antibody that binds to a known glycan bindingentity.

The bound label can be observed using any available detection method.For example, an array scanner can be employed to detect fluorescentlylabeled molecules that are bound to array. In experiments illustratedherein a ScanArray 5000 (GSI Lumonics, Watertown, Mass.) confocalscanner was used. The data from such an array scanner can be analyzed bymethods available in the art, for example, by using ImaGene imageanalysis software (BioDiscovery Inc., El Segundo, Calif.).

Methods of Detecting Disease

According to the invention, antibodies from bodily fluids of patientscan be detected using the glycan arrays of the invention. The particularglycan epitopes recognized by those antibodies are indicative of aparticular disease type. Healthy persons who do not have the disease inquestion have much lower levels of such antibodies, or substantially noantibodies that react with those glycans. Antibodies associated withdiseases such as cancer, bacterial infection, viral infection,inflammation, transplant rejection, autoimmune diseases and the like canbe detected using the glycan arrays of the invention.

For detecting disease, a test sample is obtained from a patient. Thepatient may or may not have a disease. Thus, the methods of theinvention are used to diagnose or detect whether the patient has adisease or has a propensity for developing a disease. Alternatively, themethods of the invention can be used with patients that are known tohave an identified disease. In this case, the prognosis of the diseasecan be monitored.

The test sample obtained from the patient can be any tissue, bodilyfluid sample or pathology sample. For example, the test sample can be ablood sample, a serum sample, a plasma sample, a urine sample, a breastmilk sample, an ascites fluid sample or a tissue sample. In manyembodiments, the sample is a serum sample. The test sample may or maynot contain a glycan binding entity —the methods provided herein permitdetection of whether such a glycan binding entity is present in the testsample.

In some embodiments, the presence of a particular glycan binding entityis indicative of a particular disease, condition or disease state.Hence, for example, as illustrated herein, detection of increased glycanbinding by antibodies in a patient's serum is an indicator that thepatient may have disease. Comparison of the levels of glycan bindingover time provides an indication of whether the disease is progressingor whether the patient is recovering from the disease or the disease isin remission. Hence, the invention provides methods for detectingdisease as well as monitoring the progression of disease in a patient.

A few examples of methods for detecting specific diseases or thepotential to develop disease are provided for illustrative purposes.

Breast Cancer: Breast cancer usually begins in the cells lining a breastduct and in the terminal ductal lobular unit, with the first stagethought to be excessive proliferation of individual cell(s) leading to“ductal hyperplasia.” Some of the hyperplastic cells may then becomeatypical, with a significant risk of the atypical hyperplastic cellsbecoming neoplastic or cancerous. Initially, the cancerous cells remainin the breast ducts, and the condition is referred to as ductalcarcinoma in situ (DCIS). After a time, however, these breast cancercells are able to invade tissues outside of the ductal environment,presenting the risk of metastases which can be fatal to the patient.Breast cancer proceeds through discrete premalignant and malignantcellular stages: normal ductal epithelium, atypical ductal hyperplasia,ductal carcinoma in situ (DCIS), and finally invasive ductal carcinoma.The first three stages are confined within the ductal system and,therefore, if diagnosed and treated, lead to the greatest probability ofcure.

While breast cancer through the DCIS phase is in theory quite treatable,effective treatment requires both early diagnosis and an effectivetreatment modality. At present, mammography is the state-of-the-artdiagnostic tool for detecting breast cancer. Often, however, mammographyis only able to detect tumors that have reached a size in the range from0.1 cm to 1 cm. Such a tumor mass may be reached as long as from 8 to 10years following initiation of the disease process. Detection of breastcancer at such a late stage is often too late to permit effectivetreatment.

Thus, in one embodiment, the invention provides fast, reliable andnon-invasive methods for detecting and diagnosing breast cancer in apatient. The method involves contacting a test sample from a patientwith a library or array of glycans and observing whether antibodies inthe test sample bind to selected glycans. The test sample can be anybodily fluid or tissue test sample, however, serum is readily obtainedand contains antibodies that can easily be detected using the presentmethods. Glycans to which antibodies in a serum test sample may bindinclude ceruloplasmin, Neu5Gc(2-6)GalNAc, GM1, Sulfo-T, Globo-H, andLNT-2. As a control, the pattern of glycans bound by antibodies frombreast cancer patients can be compared to the pattern of glycans boundby antibodies in serum samples from healthy, non-cancerous patients.

Viral Detection: As illustrated herein, and as further described in U.S.Provisional Application Ser. No. 60/550,667 (filed Mar. 5, 2004), ananti-HIV neutralizing antibody (2G12) binds preferentially to Man8glycans. Of all the natural high mannose type structures tested, 2G12antibodies showed a surprising and unexpectedly strong preference forbinding only the Man8 glycan. This glycan has been reported to bepresent in HIV gp120 to the extent of 20% of the total N-linked glycans(Scanlan et al. (2002) J. Virol. 76, 7306-7321). In comparison, the Man9glycan previously studied in the crystallographic work was relativelyweakly bound by 2G12, and the Man5, Man6 and Man7 glycans did notsupport binding at all.

The glycosylation of viral proteins is generally performed by host cell,rather than viral, enzymes. Given that many viral genomes are somutable, the glycosylation of viral proteins by host enzymes likelygives rise to antigenic epitopes that are more stable than the epitopesgenerated by translation of easily mutated viral nucleic acids. Hence,virally-associated glycans may form the basis of improved compositions,including vaccines, for inhibiting and treating viral infection.

Also as shown herein, influenza virus hemagglutinin binds toNeu5Acα2-3-linked to galactosides (24, 162-169, 176-180, see FIG. 7),but not to any Neu5Acα2-6- or Neu5Acα2-8-linked sialosides. Intactinfluenza viruses, such as A/Puerto Rico/8/34 (H1N1), were also stronglybound to the array. The overall affinities are consistent with previousfindings and show specificity for both α2-3 and α2-6 sialosides. Rogers,G. N. & Paulson, J. C. (1983) Virol. 127, 361-73. Influenza viruses alsobound to Neu5Acα2-3- and Neu5Acα2-6-linked to galactosides (24, 151,157, 161-180, 182-190, 199, see FIG. 7), as well as certain O-linkedsialosides.

Hence, the invention provides methods of detecting viral infection, forexample, HIV or influenza infection. The method involves contacting atest sample from a patient with a library or array of glycans andobserving whether antibodies reactive with the virus, viral antigens orthe virus itself are present in the test sample. The presence of suchantibodies, viral antigens and viral particles can be detected bydetecting their binding to glycans that have been determined topreviously bind those antibodies, viral antigens and viral particles.Hence, the glycans to which the antibodies, viral antigens or virusesbind indicate whether an infection is present. Such glycans can beviral-specific glycan epitopes or viral binding sites that are presenton host cells. For example, one type of viral-specific glycan epitope isthe Man8 glycan(s) to which the anti-HIV 2G12 antibodies bind. Detectionof antibodies that bind Man8 glycans is one indicator or HIV infectionor of progression towards development of AIDS. One of skill in the artcan readily prepare glycan arrays for screening for viral infectionusing the teachings provided herein.

Detection of Glycosylation Levels: The glycan arrays of the inventioncan also be used to detect whether various glycoproteins areappropriately glycosylated. Various diseases are characterized byinappropriate levels (e.g. lack of glycosylation) or inappropriate typesof glycosylation. For example, carbohydrate-deficient glycoproteinsyndromes (CDGS) are related to under glycosylation of proteins. Themost common initial test for CDGS is to analyze the glycosylationpattern on the glycoprotein transferrin using isoelectric focusing.According to the invention, glycans can be isolated from transferrinsamples of patients, printed on the solid surfaces described herein andquantified. Quantification can be performed using antibodies or lectinsthat bind to specific glycans. Alcoholism can also be diagnosed throughglycosylation changes of transferrin.

Detection of Transplant Rejection: As illustrated herein, immuneresponses directed against transplanted tissues were detected using thearrays and methods of the invention. In particular, several diabeticpatients received transplanted porcine fetal pancreas islet-like cellclusters. Serum was taken from these patients before transplantation andat 1 month after (t=1), 6 months after (t=2) and 12 months after (t=3)transplantation. As described and illustrated herein, significantlygreater amounts of antibodies reactive with alpha-Gal-3 glycan epitopeswere detected after transplantation (see FIG. 11). For example,antibodies in transplant recipients bound to the following glycanepitopes: Gal-alpha3-Gal-beta (structure 33),Gal-alpha3-Gal-beta4-GlcNAc[alpha3-Fucose]-beta (structure 34),Gal-alpha3-Gal-beta4-Glc-beta (structure 35),Gal-alpha3-Gal[alpha2-Fucose]-beta4-GlcNAc-beta (structure 36),Gal-alpha3-Gal-beta4-GalAc-beta (structure 37), Gal-alpha3-GalAc-alpha(structure 38), and Gal-alpha3-Gal-beta (structure 39).

In particular, antibodies were detected that bound to alpha-Gal-LeX(structure 34 in FIG. 7, also shown in FIG. 11C). This alpha-Gal-LeXglycan is not found in humans, but has been reported to be present onporcine kidney cells. See Bouhors D. et al., Gala1-3-LeX expressed oniso-neolacto ceramides in porcine kidney GLYCOCONJ. J. (10) 1001-16(1998). However, patients who received transplantation of porcine fetalpancreas islet-like cell clusters clearly exhibited an immune response(antibody production) against the alpha-Gal-LeX glycan epitopes.

Thus, the arrays and methods of the invention are useful for detecting,monitoring, evaluating and treating graft rejection aftertransplantation and/or xenotransplantation.

Methods of Treating Disease

The invention also provides glycan compositions that can be used asimmunogens and dietary supplements for treating and preventing disease.Thus, for example, the compositions of the invention can be used totreat diseases such as cancer, bacterial infection, viral infection,inflammation, transplant rejection, autoimmune diseases and the like. Insome embodiments, the glycans selected for inclusion in a composition ofthe invention are antigenic and can give rise to an immune responseagainst a bacterial species, a viral species, cancer cell type and thelike. In other embodiments, the glycans selected for inclusion in acomposition of the invention are not necessarily antigenic. Instead theglycans may bind or compete for binding to antibodies, receptors, andthe like that contribute to the prognosis of a disease. Hence, forexample, a non-antigenic glycan may be administered in order to bindantibodies that would otherwise cause tissue destruction duringinflammation or transplant rejection. In other embodiments, glycans areadministered to treat or prevent autoimmune responses.

Such compositions include one or more glycans that are typicallyrecognized by circulating antibodies associated with a disease,infection or immune condition. For example, to treat or prevent breastcancer, compositions are prepared that contain glycans that aretypically recognized by circulating antibodies of patients withmetastatic breast cancer. Examples of glycans that can be included incompositions for treating and preventing breast cancer thereforeinclude: ceruloplasmin, Neu5Gc(2-6)GalNAc, GM1, Sulfo-T, Globo-H, andLNT-2. In some embodiments, the type and amount of glycan is effectiveto provoke an anticancer cell immune response in the patient.

Similarly, compositions for preventing or treating viral infectionsinclude viral-specific glycan epitopes. For example, one type ofviral-specific glycan epitope is the Man8 glycan(s) to which theanti-HIV 2G12 antibodies bind. One of skill in the art can readilyprepare compositions of Man8 glycans, or other viral-specific glycanepitopes for treatment and prevention of many types of viral infectionsusing the teachings provided herein.

In a like manner, compositions of the invention for treating orpreventing bacterial infections include bacteria-specific glycanepitopes.

The compositions of the invention may be administered directly into thepatient, into an affected organ or systemically, or applied ex vivo tocells derived from the patient or a human cell line which aresubsequently administered to the patient, or used in vitro to select asubpopulation from immune cells derived from the patient, which are thenre-administered to the patient. The composition can be administered withan adjuvant or with immune-stimulating cytokines, such as interleukin-2.An example of an immune-stimulating adjuvant is Detox. The glycans mayalso be conjugated to a suitable carrier such as keyhole limpethaemocyanin (KLH) or mannan (see WO 95/18145 and Longenecker et al(1993) Ann. NY Acad. Sci. 690, 276-291). The glycans can be administeredto the patient orally, intramuscularly or intradermally orsubcutaneously.

In some embodiments, the compositions of the invention are administeredin a manner that produces a humoral response. Thus, production ofantibodies directed against the glycan(s) is one measure of whether asuccessful immune response has been achieved.

In other embodiments, the compositions of the invention are administeredin a manner that produces a cellular immune response, resulting in tumorcell killing by NK cells or cytotoxic T cells (CTLs). Strategies ofadministration that activate T helper cells are particularly useful. Asdescribed above, it may also be useful to stimulate a humoral response.It may be useful to co-administer certain cytokines to promote such aresponse, for example interleukin-2, interleukin-12, interleukin-6, orinterleukin-10.

It may also be useful to target the immune compositions to specific cellpopulations, for example, antigen presenting cells, either by the siteof injection, by use delivery systems, or by selective purification ofsuch a cell population from the patient and ex vivo administration ofthe glycan(s) to such antigen presenting cells. For example, dendriticcells may be sorted as described in Zhou et al (1995) Blood 86,3295-3301; Roth et al (1996) Scand. J. Immunology 43, 646-651.

A further aspect of the invention therefore provides a vaccine effectiveagainst a disease comprising an effective amount of glycans that arebound by circulating antibodies of patients with the disease.

Antibodies of the Invention

The invention provides antibodies that bind to glycans that react withcirculating antibodies present in patients with a variety of diseases.Such antibodies are useful for the diagnosis and treatment of thedisease. For example, as is illustrated herein, different patients mayhave produced different amounts and somewhat different types ofantibodies against breast-cancer associated glycan epitopes. Hence,administration of antibodies that are known to have good affinity forthe breast-cancer associated glycan epitopes of the invention will bebeneficial even though the patient has begun to produce some antibodiesreactive with breast cancer epitopes. Similarly, as illustrated herein,certain glycan molecules are excellent antigenic epitopes that arerecognized by anti-HIV neutralizing antibodies. Antibodies that haveslightly different (e.g., improved) affinities for known HIV epitopesare useful for treating and detecting HIV. Thus, the invention providesantibody preparations that can bind any of the glycan epitopes describedherein.

Antibodies can be prepared using a selected glycan, class of glycans ormixture of glycans as the immunizing antigen. The glycan or glycanmixture can be coupled to a carrier protein, if desired. Such commonlyused carrier proteins which are chemically coupled to epitopes includekeyhole limpet hemocyanin (KLH), thyroglobulin, bovine serum albumin(BSA), and tetanus toxin. A coupled protein can be used to immunize theanimal (e.g., a mouse, a rat, or a rabbit).

If desired, polyclonal or monoclonal antibodies can be further purified,for example, by binding to and elution from a matrix to which the glycanor mixture of glycans to which the antibodies were raised is bound.Those of skill in the art will know of various techniques common in theimmunology arts for purification and/or concentration of polyclonalantibodies, as well as monoclonal antibodies (Coligan, et al., Unit 9,Current Protocols in Immunology, Wiley Interscience, 1991, incorporatedby reference).

It is also possible to use the anti-idiotype technology to producemonoclonal antibodies which mimic an epitope. For example, ananti-idiotypic monoclonal antibody made to a first monoclonal antibodywill have a binding domain in the hypervariable region which is the“image” of the epitope bound by the first monoclonal antibody.

An antibody suitable for binding to a glycan is specific for at leastone portion or region of the glycan. For example, one of skill in theart can use a whole glycan or fragment of glycan to generate appropriateantibodies of the invention. Antibodies of the invention includepolyclonal antibodies, monoclonal antibodies, and fragments ofpolyclonal and monoclonal antibodies.

The preparation of polyclonal antibodies is well-known to those skilledin the art (Green et al., Production of Polyclonal Antisera, inImmunochemical Protocols (Manson, ed.), pages 1-5 (Humana Press 1992);Coligan et al., Production of Polyclonal Antisera in Rabbits, Rats, Miceand Hamsters, in Current Protocols in Immunology, section 2.4.1 (1992),which are hereby incorporated by reference). For example, a glycan orglycan mixture is injected into an animal host, preferably according toa predetermined schedule incorporating one or more boosterimmunizations, and the animal is bled periodically. Polyclonalantibodies specific for a glycan or glycan fragment may then be purifiedfrom such antisera by, for example, affinity chromatography using theglycan coupled to a suitable solid support.

The preparation of monoclonal antibodies likewise is conventional(Kohler & Milstein, Nature, 256:495 (1975); Coligan et al., sections2.5.1-2.6.7; and Harlow et al., Antibodies: A Laboratory Manual, page726 (Cold Spring Harbor Pub. 1988)), which are hereby incorporated byreference. Briefly, monoclonal antibodies can be obtained by injectingmice with a composition comprising an antigen (glycan), verifying thepresence of antibody production by removing a serum sample, removing thespleen to obtain B lymphocytes, fusing the B lymphocytes with myelomacells to produce hybridomas, cloning the hybridomas, selecting positiveclones that produce antibodies to the antigen, and isolating theantibodies from the hybridoma cultures. Monoclonal antibodies can beisolated and purified from hybridoma cultures by a variety ofwell-established techniques. Such isolation techniques include affinitychromatography with Protein-A Sepharose, size-exclusion chromatography,and ion-exchange chromatography (Coligan et al., sections 2.7.1-2.7.12and sections 2.9.1-2.9.3; Barnes et al., Purification of ImmunoglobulinG (IgG), in Methods in Molecular Biology, Vol. 10, pages 79-104 (HumanaPress 1992)). Methods of in vitro and in vivo multiplication ofmonoclonal antibodies are available to those skilled in the art.Multiplication in vitro may be carried out in suitable culture mediasuch as Dulbecco's Modified Eagle Medium or RPMI 1640 medium, optionallyreplenished by a mammalian serum such as fetal calf serum or traceelements and growth-sustaining supplements such as normal mouseperitoneal exudate cells, spleen cells, bone marrow macrophages.Production in vitro provides relatively pure antibody preparations andallows scale-up to yield large amounts of the desired antibodies. Largescale hybridoma cultivation can be carried out by homogenous suspensionculture in an air reactor, in a continuous stirrer reactor, orimmobilized or entrapped cell culture. Multiplication in vivo may becarried out by injecting cell clones into mammals histocompatible withthe parent cells, e.g., osyngeneic mice, to cause growth ofantibody-producing tumors. Optionally, the animals are primed with ahydrocarbon, especially oils such as pristine tetramethylpentadecaneprior to injection. After one to three weeks, the desired monoclonalantibody is recovered from the body fluid of the animal.

Antibodies can also be prepared through use of phage display techniques.In one example, an organism is immunized with an antigen, such as aglycan or mixture of glycans of the invention. Lymphocytes are isolatedfrom the spleen of the immunized organism. Total RNA is isolated fromthe splenocytes and mRNA contained within the total RNA is reversetranscribed into complementary deoxyribonucleic acid (cDNA). The cDNAencoding the variable regions of the light and heavy chains of theimmunoglobulin is amplified by polymerase chain reaction (PCR). Togenerate a single chain fragment variable (scFv) antibody, the light andheavy chain amplification products may be linked by splice overlapextension PCR to generate a complete sequence and ligated into asuitable vector. E. coli are then transformed with the vector encodingthe scFv, and are infected with helper phage, to produce phage particlesthat display the antibody on their surface. Alternatively, to generate acomplete antigen binding fragment (Fab), the heavy chain amplificationproduct can be fused with a nucleic acid sequence encoding a phage coatprotein, and the light chain amplification product can be cloned into asuitable vector. E. coli expressing the heavy chain fused to a phagecoat protein are transformed with the vector encoding the light chainamplification product. The disulfide linkage between the light and heavychains is established in the periplasm of E. coli. The result of thisprocedure is to produce an antibody library with up to 10⁹ clones. Thesize of the library can be increased to 10¹⁸ phage by later addition ofthe immune responses of additional immunized organisms that may be fromthe same or different hosts. Antibodies that recognize a specificantigen can be selected through panning. Briefly, an entire antibodylibrary can be exposed to an immobilized antigen against whichantibodies are desired. Phage that do not express an antibody that bindsto the antigen are washed away. Phage that express the desiredantibodies are immobilized on the antigen. These phage are then elutedand again amplified in E. coli. This process can be repeated to enrichthe population of phage that express antibodies that specifically bindto the antigen. After phage are isolated that express an antibody thatbinds to an antigen, a vector containing the coding sequences for theantibody can be isolated from the phage particles and the codingsequences can be recloned into a suitable vector to produce an antibodyin soluble form. In another example, a human phage library can be usedto select for antibodies, such as monoclonal antibodies, that bind tospecific glycan epitopes. Briefly, splenocytes may be isolated from ahuman that has a disease (e.g. cancer, bacterial infection, viralinfection, inflammation, transplant rejection, autoimmune diseases andthe like) and used to create a human phage library according to methodsdescribed herein and available in the art. These methods may be used toobtain human monoclonal antibodies that bind to specific glycanepitopes. Phage display methods to isolate antigens and antibodies areknown in the art and have been described (Gram et al., Proc. Natl. Acad.Sci., 89:3576 (1992); Kay et al., Phage display of peptides andproteins: A laboratory manual. San Diego: Academic Press (1996); Kermaniet al., Hybrid, 14:323 (1995); Schmitz et al., Placenta, 21 Suppl.A:S106 (2000); Sanna et al., Proc. Natl. Acad. Sci., 92:6439 (1995)).

An antibody of the invention may be derived from a “humanized”monoclonal antibody. Humanized monoclonal antibodies are produced bytransferring mouse complementarity determining regions from heavy andlight variable chains of the mouse immunoglobulin into a human variabledomain, and then substituting human residues in the framework regions ofthe murine counterparts. The use of antibody components derived fromhumanized monoclonal antibodies obviates potential problems associatedwith the immunogenicity of murine constant regions. General techniquesfor cloning murine immunoglobulin variable domains are described(Orlandi et al., Proc. Nat'l Acad. Sci. USA, 86:3833 (1989) which ishereby incorporated in its entirety by reference). Techniques forproducing humanized monoclonal antibodies are described (Jones et al.,Nature, 321:522 (1986); Riechmann et al., Nature, 332:323 (1988);Verhoeyen et al, Science, 239:1534 (1988); Carter et al., Proc. Nat'lAcad. Sci. USA, 89:4285 (1992); Sandhu, Crit. Rev. Biotech., 12:437(1992); and Singer et al., J. Immunol., 150:2844 (1993), which arehereby incorporated by reference).

In addition, antibodies of the present invention may be derived from ahuman monoclonal antibody. Such antibodies are obtained from transgenicmice that have been “engineered” to produce specific human antibodies inresponse to antigenic challenge. In this technique, elements of thehuman heavy and light chain loci are introduced into strains of micederived from embryonic stem cell lines that contain targeted disruptionsof the endogenous heavy and light chain loci. The transgenic mice cansynthesize human antibodies specific for human antigens (e.g. theglycans described herein), and the mice can be used to produce humanantibody-secreting hybridomas. Methods for obtaining human antibodiesfrom transgenic mice are described (Green et al., Nature Genet., 7:13(1994); Lonberg et al., Nature, 368:856 (1994); and Taylor et al., Int.Immunol., 6:579 (1994), which are hereby incorporated by reference).

Antibody fragments of the invention can be prepared by proteolytichydrolysis of the antibody or by expression in E. coli of DNA encodingthe fragment. Antibody fragments can be obtained by pepsin or papaindigestion of whole antibodies by conventional methods. For example,antibody fragments can be produced by enzymatic cleavage of antibodieswith pepsin to provide a 5S fragment denoted F(ab′)₂. This fragment canbe further cleaved using a thiol reducing agent, and optionally ablocking group for the sulfhydryl groups resulting from cleavage ofdisulfide linkages, to produce 3.5S Fab′ monovalent fragments.Alternatively, an enzymatic cleavage using pepsin produces twomonovalent Fab′ fragments and an Fc fragment directly. These methods aredescribed (U.S. Pat. Nos. 4,036,945; 4,331,647; and 6,342,221, andreferences contained therein; Porter, Biochem. J., 73:119 (1959);Edelman et al., Methods in Enzymology, Vol. 1, page 422 (Academic Press1967); and Coligan et al. at sections 2.8.1-2.8.10 and 2.10.1-2.10.4).

Other methods of cleaving antibodies, such as separation of heavy chainsto form monovalent light-heavy chain fragments, further cleavage offragments, or other enzymatic, chemical, or genetic techniques may alsobe used, so long as the fragments bind to the antigen that is recognizedby the intact antibody.

For example, Fv fragments include an association of V_(H) and V_(L)chains. This association may be noncovalent (Inbar et al., Proc. Nat'lAcad. Sci. USA, 69:2659 (1972)). Alternatively, the variable chains canbe linked by an intermolecular disulfide bond or cross-linked bychemicals such as glutaraldehyde (Sandhu, Crit. Rev. Biotech., 12:437(1992)). Preferably, the Fv fragments comprise V_(H) and V_(L) chainsconnected by a peptide linker. These single-chain antigen bindingproteins (sFv) are prepared by constructing a structural gene comprisingDNA sequences encoding the V_(H) and V_(L) domains connected by anoligonucleotide. The structural gene is inserted into an expressionvector, which is subsequently introduced into a host cell such as E.coli. The recombinant host cells synthesize a single polypeptide chainwith a linker peptide bridging the two V domains. Methods for producingsFvs are described (Whitlow et al., Methods: A Companion to Methods inEnzymology, Vol. 2, page 97 (1991); Bird et al., Science, 242:423(1988), Ladner et al., U.S. Pat. No. 4,946,778; Pack et al.,Bio/Technology, 11:1271 (1993); and Sandhu, Crit. Rev. Biotech., 12:437(1992)).

Another form of an antibody fragment is a peptide that forms a singlecomplementarity-determining region (CDR). CDR peptides (“minimalrecognition units”) can be obtained by constructing genes encoding theCDR of an antibody of interest. Such genes are prepared, for example, byusing the polymerase chain reaction to synthesize the variable regionfrom RNA of antibody-producing cells (Larrick et al., Methods: ACompanion to Methods in Enzymology, Vol. 2, page 106 (1991)).

An antibody of the invention may be coupled to a toxin. Such antibodiesmay be used to treat animals, including humans that suffer from diseasessuch as cancer, bacterial infection, viral infection, and the like. Forexample, an antibody that binds to a glycan that is etiologically linkedto development of breast cancer may be coupled to a tetanus toxin andadministered to a patient suffering from breast cancer. Similarly, anantibody that binds to a viral-specific glycan epitope may be coupled toa tetanus toxin and administered to a patient suffering from viralinfection. The toxin-coupled antibody can bind to a breast cancer cellor virus and kill it.

An antibody of the invention may be coupled to a detectable tag. Suchantibodies may be used within diagnostic assays to determine if ananimal, such as a human, has a disease or infection. Examples ofdetectable tags include, fluorescent proteins (i.e., green fluorescentprotein, red fluorescent protein, yellow fluorescent protein),fluorescent markers (i.e., fluorescein isothiocyanate, rhodamine, texasred), radiolabels (i.e., ³H, ³²P, ¹²⁵I), enzymes (i.e., β-galactosidase,horseradish peroxidase, β-glucuronidase, alkaline phosphatase), or anaffinity tag (i.e., avidin, biotin, streptavidin). Methods to coupleantibodies to a detectable tag are known in the art. Harlow et al.,Antibodies: A Laboratory Manual, page 319 (Cold Spring Harbor Pub.1988).

Dosages, Formulations and Routes of Administration

The compositions of the invention are administered to treat or preventdisease. In some embodiments, the compositions of the invention areadministered so as to achieve an immune response against the glycans inthe composition. In some embodiments, the compositions of the inventionare administered so as to achieve a reduction in at least one symptomassociated with a disease such as cancer, bacterial infection, viralinfection, inflammation, transplant rejection, autoimmune diseases andthe like.

To achieve the desired effect(s), the glycan or a combination thereof,may be administered as single or divided dosages, for example, of atleast about 0.01 mg/kg to about 500 to 750 mg/kg, of at least about 0.01mg/kg to about 300 to 500 mg/kg, at least about 0.1 mg/kg to about 100to 300 mg/kg or at least about 1 mg/kg to about 50 to 100 mg/kg of bodyweight, although other dosages may provide beneficial results. Theamount administered will vary depending on various factors including,but not limited to, what types of glycans are administered, the route ofadministration, the progression or lack of progression of the disease,the weight, the physical condition, the health, the age of the patient,whether prevention or treatment is to be achieved, and if the glycan ischemically modified. Such factors can be readily determined by theclinician employing animal models or other test systems that areavailable in the art.

Administration of the therapeutic agents (glycans) in accordance withthe present invention may be in a single dose, in multiple doses, in acontinuous or intermittent manner, depending, for example, upon therecipient's physiological condition, whether the purpose of theadministration is therapeutic or prophylactic, and other factors knownto skilled practitioners. The administration of the glycans orcombinations thereof may be essentially continuous over a preselectedperiod of time or may be in a series of spaced doses. Both local andsystemic administration is contemplated.

To prepare the composition, the glycans or antibodies or combinationsthereof are synthesized or otherwise obtained, and purified as necessaryor desired. These therapeutic agents can then be lyophilized orstabilized, their concentrations can be adjusted to an appropriateamount, and the therapeutic agents can optionally be combined with otheragents. The absolute weight of a given glycan, binding entity, antibodyor combination thereof that is included in a unit dose can vary widely.For example, about 0.01 to about 2 g, or about 0.1 to about 500 mg, ofat least one glycan, binding entity, or antibody specific for aparticular glycan can be administered. Alternatively, the unit dosagecan vary from about 0.01 g to about 50 g, from about 0.01 g to about 35g, from about 0.1 g to about 25 g, from about 0.5 g to about 12 g, fromabout 0.5 g to about 8 g, from about 0.5 g to about 4 g, or from about0.5 g to about 2 g.

Daily doses of the glycan(s), binding entities, antibodies orcombinations thereof can vary as well. Such daily doses can range, forexample, from about 0.1 g/day to about 50 g/day, from about 0.1 g/day toabout 25 g/day, from about 0.1 g/day to about 12 g/day, from about 0.5g/day to about 8 g/day, from about 0.5 g/day to about 4 g/day, and fromabout 0.5 g/day to about 2 g/day.

Thus, one or more suitable unit dosage forms comprising the therapeuticagents of the invention can be administered by a variety of routesincluding oral, parenteral (including subcutaneous, intravenous,intramuscular and intraperitoneal), rectal, dermal, transdermal,intrathoracic, intrapulmonary and intranasal (respiratory) routes. Thetherapeutic agents may also be formulated for sustained release (forexample, using microencapsulation, see WO 94/07529, and U.S. Pat. No.4,962,091). The formulations may, where appropriate, be convenientlypresented in discrete unit dosage forms and may be prepared by any ofthe methods well known to the pharmaceutical arts. Such methods mayinclude the step of mixing the therapeutic agent with liquid carriers,solid matrices, semi-solid carriers, finely divided solid carriers orcombinations thereof, and then, if necessary, introducing or shaping theproduct into the desired delivery system.

When the therapeutic agents of the invention are prepared for oraladministration, they are generally combined with a pharmaceuticallyacceptable carrier, diluent or excipient to form a pharmaceuticalformulation, or unit dosage form. For oral administration, thetherapeutic agents may be present as a powder, a granular formulation, asolution, a suspension, an emulsion or in a natural or synthetic polymeror resin for ingestion of the active ingredients from a chewing gum. Thetherapeutic agents may also be presented as a bolus, electuary or paste.Orally administered therapeutic agents of the invention can also beformulated for sustained release. For example, the therapeutic agentscan be coated, micro-encapsulated, or otherwise placed within asustained delivery device. The total active ingredients in suchformulations comprise from 0.1 to 99.9% by weight of the formulation.

By “pharmaceutically acceptable” it is meant a carrier, diluent,excipient, and/or salt that is compatible with the other ingredients ofthe formulation, and not deleterious to the recipient thereof.

Pharmaceutical formulations containing the therapeutic agents of theinvention can be prepared by procedures known in the art usingwell-known and readily available ingredients. For example, thetherapeutic agent can be formulated with common excipients, diluents, orcarriers, and formed into tablets, capsules, solutions, suspensions,powders, aerosols and the like. Examples of excipients, diluents, andcarriers that are suitable for such formulations include buffers, aswell as fillers and extenders such as starch, cellulose, sugars,mannitol, and silicic derivatives. Binding agents can also be includedsuch as carboxymethyl cellulose, hydroxymethylcellulose, hydroxypropylmethylcellulose and other cellulose derivatives, alginates, gelatin, andpolyvinyl-pyrrolidone. Moisturizing agents can be included such asglycerol, disintegrating agents such as calcium carbonate and sodiumbicarbonate. Agents for retarding dissolution can also be included suchas paraffin. Resorption accelerators such as quaternary ammoniumcompounds can also be included. Surface active agents such as cetylalcohol and glycerol monostearate can be included. Adsorptive carrierssuch as kaolin and bentonite can be added. Lubricants such as talc,calcium and magnesium stearate, and solid polyethylene glycols can alsobe included. Preservatives may also be added. The compositions of theinvention can also contain thickening agents such as cellulose and/orcellulose derivatives. They may also contain gums such as xanthan, guaror carbo gum or gum arabic, or alternatively polyethylene glycols,bentones and montmorillonites, and the like.

For example, tablets or caplets containing the therapeutic agents of theinvention can include buffering agents such as calcium carbonate,magnesium oxide and magnesium carbonate. Caplets and tablets can alsoinclude inactive ingredients such as cellulose, pre-gelatinized starch,silicon dioxide, hydroxy propyl methyl cellulose, magnesium stearate,microcrystalline cellulose, starch, talc, titanium dioxide, benzoicacid, citric acid, corn starch, mineral oil, polypropylene glycol,sodium phosphate, zinc stearate, and the like. Hard or soft gelatincapsules containing at least one therapeutic agent of the invention cancontain inactive ingredients such as gelatin, microcrystallinecellulose, sodium lauryl sulfate, starch, talc, and titanium dioxide,and the like, as well as liquid vehicles such as polyethylene glycols(PEGs) and vegetable oil. Moreover, enteric-coated caplets or tabletscontaining one or more of the therapeutic agents of the invention aredesigned to resist disintegration in the stomach and dissolve in themore neutral to alkaline environment of the duodenum.

The therapeutic agents of the invention can also be formulated aselixirs or solutions for convenient oral administration or as solutionsappropriate for parenteral administration, for instance byintramuscular, subcutaneous, intraperitoneal or intravenous routes. Thepharmaceutical formulations of the therapeutic agents of the inventioncan also take the form of an aqueous or anhydrous solution ordispersion, or alternatively the form of an emulsion or suspension orsalve.

Thus, the therapeutic agents may be formulated for parenteraladministration (e.g., by injection, for example, bolus injection orcontinuous infusion) and may be presented in unit dose form in ampoules,pre-filled syringes, small volume infusion containers or in multi-dosecontainers. As noted above, preservatives can be added to help maintainthe shelve life of the dosage form. The active agents and otheringredients may form suspensions, solutions, or emulsions in oily oraqueous vehicles, and may contain formulatory agents such as suspending,stabilizing and/or dispersing agents. Alternatively, the therapeuticagents and other ingredients may be in powder form, obtained by asepticisolation of sterile solid or by lyophilization from solution, forconstitution with a suitable vehicle, e.g., sterile, pyrogen-free water,before use.

These formulations can contain pharmaceutically acceptable carriers,vehicles and adjuvants that are well known in the art. It is possible,for example, to prepare solutions using one or more organic solvent(s)that is/are acceptable from the physiological standpoint, chosen, inaddition to water, from solvents such as acetone, ethanol, isopropylalcohol, glycol ethers such as the products sold under the name“Dowanol,” polyglycols and polyethylene glycols, C₁-C₄ alkyl esters ofshort-chain acids, ethyl or isopropyl lactate, fatty acid triglyceridessuch as the products marketed under the name “Miglyol,” isopropylmyristate, animal, mineral and vegetable oils and polysiloxanes.

It is possible to add, if necessary, an adjuvant chosen fromantioxidants, surfactants, other preservatives, film-forming,keratolytic or comedolytic agents, perfumes, flavorings and colorings.Antioxidants such as t-butylhydroquinone, butylated hydroxyanisole,butylated hydroxytoluene and α-tocopherol and its derivatives can beadded.

Additionally, the therapeutic agents are well suited to formulation assustained release dosage forms and the like. The formulations can be soconstituted that they release the active agent, for example, in aparticular part of the vascular system or respiratory tract, possiblyover a period of time. Coatings, envelopes, and protective matrices maybe made, for example, from polymeric substances, such aspolylactide-glycolates, liposomes, microemulsions, microparticles,nanoparticles, or waxes. These coatings, envelopes, and protectivematrices are useful to coat indwelling devices, e.g., stents, catheters,peritoneal dialysis tubing, draining devices and the like.

For topical administration, the therapeutic agents may be formulated asis known in the art for direct application to a target area. Formschiefly conditioned for topical application take the form, for example,of creams, milks, gels, dispersion or microemulsions, lotions thickenedto a greater or lesser extent, impregnated pads, ointments or sticks,aerosol formulations (e.g., sprays or foams), soaps, detergents, lotionsor cakes of soap. Other conventional forms for this purpose includewound dressings, coated bandages or other polymer coverings, ointments,creams, lotions, pastes, jellies, sprays, and aerosols. Thus, thetherapeutic agents of the invention can be delivered via patches orbandages for dermal administration. Alternatively, the therapeuticagents can be formulated to be part of an adhesive polymer, such aspolyacrylate or acrylate/vinyl acetate copolymer. For long-termapplications it might be desirable to use microporous and/or breathablebacking laminates, so hydration or maceration of the skin can beminimized. The backing layer can be any appropriate thickness that willprovide the desired protective and support functions. A suitablethickness will generally be from about 10 to about 200 microns.

Ointments and creams may, for example, be formulated with an aqueous oroily base with the addition of suitable thickening and/or gellingagents. Lotions may be formulated with an aqueous or oily base and willin general also contain one or more emulsifying agents, stabilizingagents, dispersing agents, suspending agents, thickening agents, orcoloring agents. The active ingredients can also be delivered viaiontophoresis, e.g., as disclosed in U.S. Pat. Nos. 4,140,122;4,383,529; or 4,051,842. The percent by weight of a therapeutic agent ofthe invention present in a topical formulation will depend on variousfactors, but generally will be from 0.01% to 95% of the total weight ofthe formulation, and typically 0.1-85% by weight.

Drops, such as eye drops or nose drops, may be formulated with one ormore of the therapeutic agents in an aqueous or non-aqueous base alsocomprising one or more dispersing agents, solubilizing agents orsuspending agents. Liquid sprays are conveniently delivered frompressurized packs. Drops can be delivered via a simple eyedropper-capped bottle, or via a plastic bottle adapted to deliver liquidcontents dropwise, via a specially shaped closure.

The therapeutic agent may further be formulated for topicaladministration in the mouth or throat. For example, the activeingredients may be formulated as a lozenge further comprising a flavoredbase, usually sucrose and acacia or tragacanth; pastilles comprising thecomposition in an inert base such as gelatin and glycerin or sucrose andacacia; and mouthwashes comprising the composition of the presentinvention in a suitable liquid carrier.

The pharmaceutical formulations of the present invention may include, asoptional ingredients, pharmaceutically acceptable carriers, diluents,solubilizing or emulsifying agents, and salts of the type that areavailable in the art. Examples of such substances include normal salinesolutions such as physiologically buffered saline solutions and water.Specific non-limiting examples of the carriers and/or diluents that areuseful in the pharmaceutical formulations of the present inventioninclude water and physiologically acceptable buffered saline solutionssuch as phosphate buffered saline solutions pH 7.0-8.0.

The active ingredients of the invention can also be administered to therespiratory tract. Thus, the present invention also provides aerosolpharmaceutical formulations and dosage forms for use in the methods ofthe invention.

In general, such dosage forms comprise an amount of at least one of theagents of the invention effective to treat or prevent the clinicalsymptoms of a disease. Diseases contemplated by the invention include,for example, cancer, bacterial infection, viral infection, inflammation,transplant rejection, autoimmune diseases and the like. Anystatistically significant attenuation of one or more symptoms of adisease is considered to be a treatment of the disease.

Alternatively, for administration by inhalation or insufflation, thecomposition may take the form of a dry powder, for example, a powder mixof the therapeutic agent and a suitable powder base such as lactose orstarch. The powder composition may be presented in unit dosage form in,for example, capsules or cartridges, or, e.g., gelatin or blister packsfrom which the powder may be administered with the aid of an inhalator,insufflator, or a metered-dose inhaler (see, for example, thepressurized metered dose inhaler (MDI) and the dry powder inhalerdisclosed in Newman, S. P. in Aerosols and the Lung, Clarke, S. W. andDavia, D. eds., pp. 197-224, Butterworths, London, England, 1984).

Therapeutic agents of the present invention can also be administered inan aqueous solution when administered in an aerosol or inhaled form.Thus, other aerosol pharmaceutical formulations may comprise, forexample, a physiologically acceptable buffered saline solutioncontaining between about 0.1 mg/ml and about 100 mg/ml of one or more ofthe therapeutic agents of the present invention specific for theindication or disease to be treated. Dry aerosol in the form of finelydivided solid therapeutic agent that are not dissolved or suspended in aliquid are also useful in the practice of the present invention.Therapeutic agents of the present invention may be formulated as dustingpowders and comprise finely divided particles having an average particlesize of between about 1 and 5 μm, alternatively between 2 and 3 μm.Finely divided particles may be prepared by pulverization and screenfiltration using techniques well known in the art. The particles may beadministered by inhaling a predetermined quantity of the finely dividedmaterial, which can be in the form of a powder. It will be appreciatedthat the unit content of active ingredient or ingredients contained inan individual aerosol dose of each dosage form need not in itselfconstitute an effective amount for treating the particular immuneresponse, vascular condition or disease since the necessary effectiveamount can be reached by administration of a plurality of dosage units.Moreover, the effective amount may be achieved using less than the dosein the dosage form, either individually, or in a series ofadministrations.

For administration to the upper (nasal) or lower respiratory tract byinhalation, the therapeutic agents of the invention are convenientlydelivered from a nebulizer or a pressurized pack or other convenientmeans of delivering an aerosol spray. Pressurized packs may comprise asuitable propellant such as dichlorodifluoromethane,trichlorofluoromethane, dichlorotetrafluoroethane, carbon dioxide orother suitable gas. In the case of a pressurized aerosol, the dosageunit may be determined by providing a valve to deliver a metered amount.Nebulizers include, but are not limited to, those described in U.S. Pat.Nos. 4,624,251; 3,703,173; 3,561,444; and 4,635,627. Aerosol deliverysystems of the type disclosed herein are available from numerouscommercial sources including Fisons Corporation (Bedford, Mass.),Schering Corp. (Kenilworth, N.J.) and American Pharmoseal Co.,(Valencia, Calif.). For intra-nasal administration, the therapeuticagent may also be administered via nose drops, a liquid spray, such asvia a plastic bottle atomizer or metered-dose inhaler. Typical ofatomizers are the Mistometer (Wintrop) and the Medihaler (Riker).

Furthermore, the active ingredients may also be used in combination withother therapeutic agents, for example, pain relievers, anti-inflammatoryagents, other anti-cancer agents and the like, whether for theconditions described or some other condition.

Kits

The present invention further pertains to a packaged pharmaceuticalcomposition such as a kit or other container for detecting, controlling,preventing or treating a disease. The kits of the invention can bedesigned for detecting, controlling, preventing or treating diseasessuch as cancer, bacterial infection, viral infection, inflammation,transplant rejection, autoimmune diseases and the like. In oneembodiment, the kit or container holds an array or library of glycansfor detecting disease and instructions for using the array or library ofglycans for detecting the disease. The array includes at least oneglycan that is bound by antibodies present in serum samples of personswith the disease.

In another embodiment, the kit or container holds a therapeuticallyeffective amount of a pharmaceutical composition for treating,preventing or controlling a disease and instructions for using thepharmaceutical composition for control of the disease. Thepharmaceutical composition includes at least one glycan of the presentinvention, in a therapeutically effective amount such that the diseaseis controlled, prevented or treated.

In a further embodiment, the kit comprises a container containing anantibody that specifically binds to a glycan that is associated with adisease. The antibody can have a directly attached or indirectlyassociated therapeutic agent. The antibody can also be provided inliquid form, powder form or other form permitting ready administrationto a patient.

The kits of the invention can also comprise containers with tools usefulfor administering the compositions of the invention. Such tools includesyringes, swabs, catheters, antiseptic solutions and the like.

The following examples are for illustration of certain aspects of theinvention and is not intended to be limiting thereof.

EXAMPLE 1 Enzymatic Synthesis of Glycans

The inventors have previously cloned and characterized the bacterial N.meningitides enzymes β4GalT-GalE and β3GlcNAcT. Blixt, O.; Brown, J.;Schur, M.; Wakarchuk, W. and Paulson, J. C., J. Org. Chem. 2001, 66,2442-2448; Blixt, O.; van Die, I.; Norberg, T. and van den Eijnden, D.H., Glycobiol. 1999, 9, 1061-1071. β4GalT-GalE is a fusion proteinconstructed from β4GalT and theuridine-5′-diphospho-galactose-4′-epimerase (GalE) for in situconversion of inexpensive UDP-glucose to UDP-galactose providing a costefficient strategy.

Both enzymes, β4GalT-GalE and β3GlcNAcT, were over expressed in E. coliAD202 in a large-scale fermentor (100 L). Bacteria were cultured in 2YTmedium and induced with iso-propyl-thiogalactopyranoside (IPTG) toultimately produce 8-10 g of bacterial cell paste/L cell media. Theenzymes were then released from the cells by a microfluidizer and weresolubilized in Tris buffer (25 mM, pH 7.5) containing manganese chloride(10 mM) and Triton X (0.25%) to reach enzymatic activities of about 50U/L and 115 U/L of cell culture β4GalT-GalE and β3GlcNAcT, respectively.

Specificity studies of the β3GlcNAcT (Table 4) revealed that lactose (4)is the better acceptor substrate (100%) while the enzyme shows justabout 7-8% activity with N-acetyllactosamine (6). The structures ofthese disaccharides are provided below.

Adding the hydrophobic para-nitrophenyl ring as an aglycon to thereducing end of the acceptors enhanced the activity of the enzyme up to10 fold (compare 4 with 5 and 6 with 7). The increase in the enzymeactivity by adding a hydrophobic aglycon to the acceptor sugar, thoughto the lesser extent, has also been shown for β4GalT (compare 12 with13, 14). The relaxed substrate specificity of these enzymes makes themvery useful for preparative synthesis of various carbohydratestructures, including poly-N-acetyllactosamines. TABLE 4 Selectedβ4GalT-GalE and β3GlcNAcT Specificity Data Acceptor Relative enzymeactivity (%) β(1-3)GlcNAcT-activity^(#)  1 Gal 5  2 Galα-OpNP 102  3Galβ-OpNP 16  4 Galβ(1-4)Glc 100  5 Galβ(1-4)Glcβ-OpNP 945  6Galβ(1-4)GlcNAc 7  7 Galβ(1-4)GlcNAcβ-OpNP 74  8 Galβ(1-3)GlcNAc 5β(1-4)GalT-GalE-activity*  9 Glc 80 10 Glcβ-OpNP 60 11 GlcNH₂ 30 12GlcNAc 100 13 GlcNAcβ-OpNP 120 14 GlcNAcβ-Osp₆ 360 15 GlcNAllocβ-sp₇ 550Abbreviations:pNP, para-nitrophenyl;sp₆, 2-azidoethyl;sp₇, 5-azido-3-oxapentyl,Alloc, allyloxycarbonyl

Poly-N-acetyllactosamine is a unique carbohydrate structure composed ofN-acetyllactosamine repeats that provides the backbone structure foradditional modifications, such as sialylation and/or fucosylation. Theseextended oligosaccharides have been shown to be involved in variousbiological functions by interacting as a specific ligand to selectins orgalectins. Ujita, M.; McAuliffe, J.; Hindsgaul, O.; Sasaki, K.; Fukuda,M. N. and Fukuda, M., J. Biol. Chem. 1999, 274, 16717-16726; Appelmelk,B. J.; Shiberu, B.; Trinks, C.; Tapsi, N.; Zheng, P. Y.; Verboom, T.;Maaskant, J.; Hokke, C. H.; Schiphorst, W. E. C. M.; Blanchard, D.;SimoonsSmit, I. M.; vandenEijnden, D. H. and Vandenbroucke Grauls, C. M.J. E., Infect. Immun. 1998, 66, 70-76; Leppaenen, A.; Penttilae, L.;Renkonen, O.; McEver, R. P. and Cummings, R. D., J. Biol. Chem. 2002,277, 39749-39759; Renkonen, O., Cell. Mol Life Sci. 2000, 57, 1423-1439;Baldus, S. E.; Zirbes, T. K.; Weingarten, M.; Fromm, S.; Glossmann, J.;Hanisch, F. G.; Monig, S. P.; Schroder, W.; Flucke, U.; Thiele, J.;Holscher, A. H. and Dienes, H. P., Tumor Biology. 2000, 21, 258-266;Cho, M. and Cummings, R. D., TIGG. 1997, 9, 47-56, 171-178.

Based on the specificity data in Table 4, enzymatic synthesis ofgalactosides and polylactosamines can be performed in multi-gramquantities. This method employed various fucosyltransferases (FUTs).Several fucosyltransferases (FUTs) have been characterized in terms ofsubstrate specificities and biological functions in differentlaboratories. Murray, B. W.; Takayama, S.; Schultz, J. and Wong, C. H.,Biochem. 1996, 35, 11183-11195; Weston, B. W.; Nair, R. P.; Larsen, R.D. and Lowe, J. B., J. Biol. Chem. 1992, 267, 4152-4160; Kimura, H.;Shinya, N.; Nishihara, S.; Kaneko, M.; Irimura, T. and Narimatsu, H.,Biochem. Biophys. Res. Comm. 1997, 237, 131-137; Chandrasekaran, E. V.;Jain, R. K.; Larsen, R. D.; Wlasichuk, K. and Matta, K. L., Biochem.1996, 35, 8914-8924; Devries, T.; Vandeneijnden, D. H.; Schultz, J. andOneill, R., FEBS Lett. 1993, 330, 243-248; Devries, T. and van denEijnden, D. H., Biochem. 1994, 33, 9937-9944

The available specificity data in combination with large scaleproduction of recombinant FUTs made it possible to synthesize variousprecious fucosides in multigram quantities. Scheme I illustrates thegeneral procedure employed for elongating the poly-LacNAc backbone andselected fucosylated structures using different FUTs and GDP-fucose.

A systematic gram-scale synthesis of different fucosylated lactosaminederivatives was initiated using the Scheme I and the followingrecombinant fucosyltransferases, FUT-II, FUT-III, FUT-IV, FUT-V, andFUT-VI. All the above fucosyltransferases, except for FUT-V, wereproduced in the insect cell expression system and either partiallypurified on a GDP-sepharose affinity column or concentrated in aTangential Flow Filtrator (TFF-MWCO 10k) as a crude enzyme mixture. TheFUT-V enzyme was expressed in A. niger as described in Murray, B. W.;Takayama, S.; Schultz, J. and Wong, C. H., Biochem. 1996, 35,11183-11195.

The yields for different stages of production of the fucosylatedlactosamine derivatives were 75-90% for LeX (2 enzymatic steps), 45-50%for dimeric LacNAc structures (4 enzymatic steps) and 30-35% fortrimeric lacNAc structures (6 enzymatic steps).

EXAMPLE 2 Synthesis of Sialic-acid-containing Oligosaccharides

Sialic acid is a generic designation used for 2-keto-3-deoxy-nonulosonicacids. The most commonly occurring derivatives of this series ofmonosaccharides are those derived from N-acetylneuraminic acid (Neu5Ac),N-glycolylneuraminic acid (Neu5Gc) and the non-aminated3-deoxy-D-glycero-D-galacto-2-nonulosonic acid (KDN).Sialic-acid-containing oligosaccharides are an important category ofcarbohydrates that are involved in different biological regulations andfunctions. Sialic acids are shown to be involved in adsorption oftoxins/viruses, and diverse cellular communications through interactionswith carbohydrate binding proteins (CBPs). Selectins and Siglecs (sialicacid-binding immunoglobulin-superfamily lectins) are among thosewell-characterized CBPs that function biologically through sialic acidinteractions.

Synthesis of oligosaccharides containing sialic acids is not trivial.Unfortunately, the chemical approaches have several hampering factors incommon. For example, stereo selective glycosylation with sialic acidgenerally gives an isomeric product, and as a result, purificationproblems and lower yields. Its complicated nature, also requireextensive protecting group manipulations and careful design of bothacceptor and donor substrates and substantial amounts of efforts areneeded to prepare these building blocks.

For a fast and efficient way to sialylate carbohydrate structures, themethod of choice is through catalysis by sialyltransferases. Enzymaticsialylation generating Neu5Ac-containing oligosaccharides is way togenerate sialylate carbohydrates for both analytical and preparativepurposes. Koeller, K. M. and Wong, C.-H., Nature 2001, 409, 232-240;Gilbert, M.; Bayer, R.; Cunningham, A.-M.; DeFrees, S.; Gao, Y.; Watson,D. C.; Young, N. M. and Wakarchuk, W. W., Nature Biotechnol. 1998, 16,769-772; Ichikawa, Y.; Look, G. C. and Wong, C. H., Anal. Biochem. 1992,202, 215-238. However, efficient methods for preparation ofoligosaccharides having the Neu5Gc or KDN structures have not previouslybeen explored to the same extent because of the scarcity of thesesialoside derivatives.

A simple way to obtain different sialoside derivatives was devised usinga modification of a method, originally developed by Wong and co-workers.Crocker, P. R., Curr. Opin. Struct. Biol. 2002, 12, 609-615. This methodemployed recombinant sialyltransferases along with a commercial Neu5Acaldolase, ST3-CMP-Neu5Ac synthetase. Gilbert, M.; Bayer, R.; Cunningham,A.-M.; DeFrees, S.; Gao, Y.; Watson, D. C.; Young, N. M. and Wakarchuk,W. W., Nature Biotechnol. 1998, 16, 769-772.

The preferred route to generate Neu5Ac-oligosaccharides was to use aone-pot procedure described in Scheme II (B and C).

Briefly, ST3-CMP-Neu5Ac synthetase catalyzed the formation of CMP-Neu5Acquantitatively from 1 equivalent of Neu5Ac and 1 equivalent of CTP.After removal of the fusion protein by membrane filtration (MW cut-off10k) a selected galactoside and a recombinant sialyltransferase asdescribed in Table 5 was introduced to produce the desiredNeu5Ac-sialoside. TABLE 5 Recombinant Sialyltransferases Produced forSynthesis Produced Sialyltransferase Source of Production Activity*hST6Gal-I Baculovirus (19) 20 pST3Gal-I Baculovirus (45) 20 rST3Gal-IIIA. Niger ^(#) 50 chST6Gal-I Baculovirus (46) 10 ST3Gal-Fusion E. coli(42) 6000 ST8 (Cst-II) E. coli (70) 140*Units/L cell cultureThis synthetic scheme produced multi-gram quantities of producttypically with a yield of 70-90% recovery of sialylated products.

To synthesize Neu5Gc and KDN derivatives the one-pot system wouldinclude another enzymatic reaction in addition to routes B and C (SchemeII). In this respect, mannose derivatives, pyruvate (3 eqv.) andcommercial microorganism Neu5Ac aldolase (Toyobo) were introduced intothe one-pot half-cycle (Scheme II, A). The enzymes in Table 5 were ableto generate various N- and O-linked oligosaccharides with α(2-3)-,α(2-6)- or α(2-8)-linked sialic acid derivatives of Neu5Gc, KDN and someof the 9-azido-9deoxy-Neu5Ac-analogs in acceptable yields (45-90%).O-linked sialyl-oligosaccharides are another class of desired compoundsfor the biomedical community. These structures are frequently found invarious cancer tissues and lymphoma and are highly expressed in manytypes of human malignancies including colon, breast, pancreas, ovary,stomach, and lung adenocarcinomas. Dabelsteen, E., J. Pathol. 1996, 179,358-369; Itzkowitz, S. H.; Yuan, M.; Montgomery, C. K.; Kjeldsen, T.;Takahashi, H. K. and Bigbee, W. L., Cancer Res. 1989, 49, 197-204.

The inventors have previously reported the cloning, expression, andcharacterization of chicken ST6GalNAc-I and its use in preparativesynthesis of the O-linked sialoside antigens, STn-, α(2-6)SiaT-,α(2-3)SiaT- and Di-SiaT-antigen. Blixt, O.; Allin, K.; Pereira, L.;Datta, A. and Paulson, J. C., J. Am. Chem. Soc. 2002, 124, 5739-5746.Briefly, the recombinant enzyme was expressed in insect cells andpurified by CDP-sepharose affinity chromatography to generateapproximately 10 U/L of cell culture. The enzymatic activity wasevaluated on a set of small acceptor molecules (Table 6), and it wasfound that an absolute requirement for enzymatic activity is that theanomeric position on GalNAc is α-linked to threonine. TABLE 6chST6GalNAc-I Activity of α-D-Galacto Derivatives

Compound R₁ R₂ R₃ R₄ R₅ cpm nmol/mg × min⁻¹ D-GalNAc H NHAc   0 0.00 1 HNHAc N₃ H H  65 0.06 2 H NHAc NHAc H H  121 0.11 3c H NHAc NHAc COOCH₃CH₃ 9133 8.60 4 H N₃ NHAc COOCH₃ CH₃ 3043 2.90 5 H NH₂ NHAc COOCH₃ CH₃1421 1.30 6 H NHAc NHF_(moc) COOCH₃ CH₃ 13277  12.50* 7c Galβ1,3 NHAcNHAc COOCH₃ CH₃ 12760  12.00 NOTE:*Product was isolated by using Sep-Pak (C18) cartridges as described inPalcic, M. M.; Heerze, L. D.; Pierce, M. and Hindsgaul, O., Glycoconj.J. 1988, 5, 49-63.

Thus, O-linked sialosides terminating with a protected threonine couldsuccessfully be synthesized on gram-scale reactions using Scheme IV. Tobe able to attach these compounds to other functional groups, theN-acetyl protecting group on threonine could be substituted with aremovable 9-fluorenyl (F-moc) derivative before enzymatic extension withchST6GalNAc-I. Blixt, O.; Collins, B. E.; Van Den Nieuwenhof, I. M.;Crocker, P. R. and Paulson, J. C., (2003 J. Biol. Chem. 15: 278). Asseen in Table 6, the enzyme was not sensitive to bulky groups at thisposition (compound 6).

EXAMPLE 3 Synthesis of Ganglioside Mimics

Gangliosides are glycolipids that comprise a structurally diverse set ofsialylated molecules. They are attached and enriched in nervous tissuesand they have been found to act as receptors for growth factors, toxinsand viruses and to facilitate the attachment of human melanoma andneuroblastoma cells. Kiso, M., Nippon Nogei Kagaku Kaishi. 2002, 76,1158-1167; Gagnon, M. and Saragovi, H. U., Expert Opinion on TherapeuticPatents. 2002, 12, 1215-1223; Svennerholm, L., Adv. Gen. 2001, 44,33-41; Schnaar, R. L., Carbohydr. Chem. Biol. 2000, 4, 1013-1027;Ravindranath, M. H.; Gonzales, A. M.; Nishimoto, K.; Tam, W.-Y.; Soh, D.and Morton, D. L., Ind. J. Exp. Biol. 2000, 38, 301-312; Rampersaud, A.A.; Oblinger, J. L.; Ponnappan, R. K.; Burry, R. W. and Yates, A. J.,Biochem. Soc. Trans. 1999, 27, 415-422; Nohara, K., Seikagaku. 1999, 71,337-341.

Despite the importance of these sialylated ganglioside structures,methods for their efficient preparation have been limiting. Theintroduction of sialic acid to a glycolipid core structure have shown tobe a daunting task, needed complicated engineering with well executedsynthetic strategies.

Recently, several glycosyltransferase genes from Campylobacter jejuni(OH4384) have been identified to be involved in producing variousganglioside-related lipoligosaccharides (LOS) expressed by thispathogenic bacteria. Gilbert, M.; Brisson, J.-R.; Karwaski, M.-F.;Michniewicz, J.; Cunningham, A.-M.; Wu, Y.; Young, N. M. and Wakarchuk,W. W., J. Biol. Chem. 2000, 275, 3896-3906. Among these genes, cst-II,coding for a bifunctional α(2-3/8) sialyltransferase, has beendemonstrated to catalyze transfers of Neu5Ac α(2-3) and α(2-8) tolactose and sialyllactose, respectively. Another gene, cgtA, coding fora β(1-4)-N-acetylgalactosaminyltransferase (β4GalNAcT) that is reportedto transfer GalNAc β(1-4) to Neu5Acα(2-3)lactose acceptors generatingthe GM2 (Neu5Acα(2-3)[GalNAcβ(1-4)]Galβ(1-4)Glc-) epitope.

The gene products of the two glycosyltransferase genes (cst-II and cgtA)were successfully over expressed in large scale (100 L E. colifermentation) and used in the preparative synthesis of variousganglioside mimics. For synthetic purposes an extensive specificitystudy of these enzymes was also conducted using neutral and sialylatedstructures to further specify the synthetic utility of these enzymes.

For a cost-efficient synthesis of GalNAc-containing oligosaccharides,expensive uridine-5′-diphosphate-N-acetylgalactosamine (UDP-GalNAc) wasproduced in situ from inexpensive UDP-GlcNAc by theUDP-GlcNAc-4′-epimerase (GalNAc-E). GalNAc-E was cloned from rat liverinto the E. coli expression vector (pCWori) and expressed in E. coliAD202 cells. Briefly, a lactose derivative was elongated with sialicacid repeats using α(2-8)-sialyltransferase and crude CMP-Neu5Ac.Several products (GM3, GD3, GT3) were isolated from this mixture.Increasing CDP-Neu5Ac from 2.5 to 4 equivalents favors the formation ofGT3, and minor amounts of GD3 were isolated. Typical yields range from40-50% of the major compound and 15-20% for the minor compound. Isolatedcompounds were further furbished with the action of GM2-synthetase(CgtA) and GalE to give the corresponding GM2, GD2, and GT2 structuresin quantitative yields (Scheme V).

Therefore, methodologies were developed for generating diverse series ofglycans, such as poly-N-acetyllactosamine and its correspondingfucosylated and/or sialylated compounds, various sialoside derivativesof N- and O-linked glycans, and ganglioside mimic structures.Furthermore, a simple route to produce the scarce sialic acidderivatives was described. This work demonstrates that chemoenzymaticsynthesis of complicated carbohydrate structures can reach a facile andpractical level by employing a functional toolbox of differentglycosyltransferases. Detailed information of the specificity of theseenzymes is needed for developing a library of glycan compounds with anextensive structural assortment. The invention provides such a libraryof carbohydrates and methods for using the library in high throughputstudies of carbohydrate-protein, as well as, carbohydrate-carbohydrateinteractions.

EXAMPLE 4 Isolating Glycans from Natural Sources

The Example illustrates how certain type of mannose-containing glycanscan be isolated from bovine pancreatic ribonuclease B.

Pronase Digestion of Bovine Pancreatic Ribonuclease B: Bovine pancreaticribonuclease B (Sigma Lot 060K7650) was dissolved in buffer (0.1M Tris+1mM MgCl₂+1 mM CaCl₂ pH 8.0) and pronase (Calbiochem Lot B 50874) wasadded to give a ratio by weight of five parts glycoprotein to one partpronase. It was incubated at 60° C. for 3 hours. Mannose-containingglycans in the digested sample were affinity purified using a freshlyprepared Con A in buffer (0.1M Tris, 1 mM MgCl₂, 1 mM CaCl₂, pH 8.0),washed and eluted with 200 mls 0.1M methyl-a-D-mannopyranoside(Calbiochem Lot B37526). The Con A eluted sample was purified onCarbograph solid-phase extraction column (Alltech 1000 mg, 15 ml) andeluted with 30% acetonitrile +0.06% TFA. It was dried and reconstitutedin 1 ml water. Mass analysis was done by MALDI and glycan quantificationby phenol sulfuric acid assay.

The pronase digested ribonuclease b was diluted with 5 mls 0.1M Tris pH8.0 loaded onto 15 mls Con A column in 0.1M Tris, 1 mM MgCl₂, 1 mMCaCl₂, pH 8.0, washed and eluted with 50 mls 0.1M methyl-α-Dmannopyranoside. It was then purified on Carbograph solid-phaseextraction column (Alltech 1000 mg, 15 ml) eluted with 80% acetonitrile,containing 0.1% TFA, dried and reconstituted in 2 ml water. Massanalysis and glycan quantification were performed using a Voyager EliteMALDI-TOF (Perseptive BioSystems) in negative mode.

Separation of Fractions on Dionex: Pronase digested ribonuclease b wasinjected on the DIONEX using a PA-100 column and eluted with thefollowing gradient: Solution A=0.1M NaOH, B=0.5M NaOAc in 0.1M NaOH; 0%B for 3 mins, then a linear gradient from 0% B to 6.7% B in 34 mins. Theindividual peak fractions were collected and purified on Carbographsolid-phase columns (Alltech 150 mg, 4 ml) by eluting with 80%acetonitrile containing 0.1% TFA. They were dried and reconstituted inwater. Final Mass analysis and glycan quantification were performed.

EXAMPLE 5 Preparation and Use of Glycan Arrays

Materials. Natural glycoproteins, alphal-acid glycoprotein (α₁-AGP),α₁-AGP glycoform A and B were prepared as described in Shiyan, S. D. &Bovin, N. V. (1997) Glycoconj. J. 14, 631-8. Ceruloplasmin, fibrinogen,and apo-transferrin were obtained from Sigma-Aldrich Chemical Company,MO. Synthetic glycan ligands 7-134, 146-200 (structures shown in FIG. 7)were from The Consortium for Functional Glycomics or prepared asdescribed in Pazynina et al. (2003) Mendeleev Commun. 13, 245-248;Pazynina et al. (2002) Mendeleev Commun. 12, 183-184; Pazynina et al.(2002) Tet. Lett. 43, 8011-8013; Nifant'ev et al. (1996) J. Carbohydr.Chem. 15, 939-953; Zemlyanukhina et al. (1995) Carbohydr. Lett. 1,277-284. Ligands 111, 135-139 (shown in FIG. 7) were obtained throughone-pot chemical synthesis as described in Lee et al. (2004) Angew.Chem. Int. Ed. 43, 1000-1003. Ligands 140-145 (shown in FIG. 7) wereisolated from ribonuclease as described herein.

NHS-activated glass slides (Slide-H) were employed that were from SchottNexterion (Germany). These slides are coated with a hydrogel, which iscomposed of a multi-component coating matrix (thickness: 10-60 nm),which is cross-linked with the microarray glass substrate allowingstringent washing steps. Long, hydrophilic polymer spacers tether thefunctional groups (amine-reactive N-hydroxysuccinimide-esters) to thecoating matrix, thereby ensuring that immobilized probes are highlyaccessible in a flexible, solution-like environment. The roboticprinting arrayer employed was custom made by Robotic Labware Designs(Carlsbad, Calif.). Arrays were printed using CMP4B microarray spottingpins (TeleChem International, Inc).

Several glycan binding proteins (GBPs) were obtained from commercialsources (Con A and ECA from EY-laboratories Inc., San Mateo, Calif.;anti-CD15 from BD Biosciences, San Jose, Calif.). Other types of glycanbinding proteins were obtained from various investigators includingDC-SIGN (van Die et al. (2003) Glycobiology 13, 471-478), Influenzavirus, A/Puerto Rico/8/34 (H1N1) (Gamblin et al. (2004) Science 303,1838-42), 2G12 (Calarese et al. (2003) Science 300, 2065-71),Cyanovirin-N (Scanlan et al. (2002) J. Virol. 76, 7306-21), H3 HA(Stevens, Blixt and Wilson; manuscript in preparation).

Human serum was obtained from healthy volunteers at The General ClinicalResearch Center, Scripps Hospital, La Jolla. Human saliva was similarlyobtained from a healthy volunteer. The samples were centrifuged for 30mins at 3000 rpm and heat inactivated at 56° C. for 25 minutes. CD22 wasexpressed and purified as described in Blixt et al. (2003) J. Biol.Chem. 278, 31007-19. Recombinant human Galectin-4 was also prepared asdescribed for rat Galectin-4 by Huflejt et al. (1997) J. Biol. Chem.272, 14294-303. Galectin-4-AlexaFluor488 was made with AlexaFluor488protein labeling Kit from Molecular Probes according to themanufacturer's instructions. Rabbit anti-CVN was obtained as describedin Scanlan et al. (2002) J. Virol. 76, 7306-21. Monoclonal mouseanti-human-IgG-IgM-IgA-Biotin antibody and Streptavidin-FITC were fromPierce, Rockford, Ill. Rabbit anti-goat-IgG-FITC, goatanti-human-IgG-FITC, mouse anti-HisTag-IgG-Alexafluor-488 andanti-mouse-IgG-Alexafluor-488 were purchased from Vector Labs(Burlingame, Calif.). Rabbit anti-Influenza virus A/PR/8/34 was from theWorld Influenza Centre, Mill Hill, London, UK. Other reagents andconsumables were from commercial sources with highest possible quality.

Pronase Digestion of Bovine Pancreatic Ribonuclease B. 540 mg of bovinepancreatic ribonuclease b (Sigma Lot 060K7650) was dissolved in 5 mls of0.1M Tris+1 mM MgCl₂+1 mM CaCl₂ pH 8.0. 108 mg of pronase (CalbiochemLot B 50874) was added to give a ratio by weight of five partsglycoprotein to one part pronase. This mixture was incubated at 60° C.for 3 hours. A second dose of 108 mg pronase was added and incubated at37° C. for another 3 hours, after which it was boiled for 30 minutes,cooled and centrifuged. The sample was loaded onto 20 ml of freshlyprepared ConA in 0.1M Tris, 1 mM MgCl₂, 1 mM CaCl₂, pH 8.0, washed andeluted with 200 ml 0.1M methyl-α-D-mannopyranoside (Calbiochem LotB37526). The Con A eluted sample was purified on Carbograph solid-phaseextraction column (Alltech 1000 mg, 15 ml) and eluted with 30%acetonitrile+0.06% TFA. The eluate was dried and reconstituted in lmlwater. Mass analysis was done by MALDI and glycan quantification byphenol sulfuric acid assay.

Carbohydrates obtained from bovine pancreatic ribonuclease B wereseparated by DIONEX chromatography. 20 ul of the pronase digestedribonuclease b was injected on the DIONEX using a PA-100 column andeluted with the following gradient (solution A=0.1M NaOH, solutionB=0.5M NaOAc in 0.1M NaOH): 0% B for 3 min, then a linear gradient from0% B to 6.7% B for 34 min. The individual peak fractions were collectedand purified on Carbograph solid-phase columns (Alltech 150 mg, 4 ml) byelution with 80% acetonitrile containing 0.1% TFA. The peak fractionswere then dried and reconstituted in water. Final Mass analysis andglycan quantification were performed.

Glycan array fabrication. Microarrays were printed by robotic pindeposition of ˜0.6 nL of various concentrations (10-100 μM) ofamine-containing glycans in print buffer (300 mM phosphate, pH 8.5containing 0.005% Tween-20) onto NHS-activated glass slides. Eachcompound was printed at two concentrations (100 μM and 10 μM) and eachconcentration in a replicate of six. Printed slides were allowed toreact in an atmosphere of 80% humidity for 30 mins followed bydesiccation over night. Remaining NHS-groups were blocked by immersionin buffer (50 mM ethanolamine in 50 mM borate buffer, pH 9.2) for 1 hr.Slides were rinsed with water, dried and stored in desiccators at roomtemperature prior to use.

Glycan Binding Protein binding assay. Printed slides were analyzedwithout any further modification of the surface. Slides were incubatedin either a one step procedure with labeled proteins, or a sandwichprocedure in which the slide was first incubated with a sample thatmight contain a glycan binding protein (GBP) and then was overlaid withlabeled secondary antibodies or GBP's pre-complexed with labeledantibodies. GBP's were added at a concentration of 5-50 μg/mL in buffer(usually PBS containing 0.005-0.5% Tween-20). Secondary antibodies (10μg/mL in PBS) were overlaid on bound GBP. GBP-antibody pre-complexeswere prepared in a molar ratio of 1:0.5:0.25 (5-50 μg/mL) for GBP: 2°antibody: 3° antibody, respectively (15 mins on ice). The samples(50-100 μL) were applied either directly onto the surface of a singleslide and covered with a microscope cover slip, or applied between twoparallel slides separated by thin tape and pressed together by paperclips (see Ting et al. (2003) BioTechniques 35, 808-810) and thenincubated in a humidified chamber for 30-60 minutes. Slides weresubsequently washed by successive rinses in (i) PBS-Tween (0.05%), (ii)PBS and (iii) de-ionized water, then immediately subjected to imaging.Serum samples were typically used at dilutions of 1:25 and 0.4-0.8 mLapplied directly onto the slide surface without any cover glass. Salivasamples were similarly handled. The slides were gently rocked at roomtemperature for 90 min followed by detection with secondary antibodies(Table 7). Whole virus was applied (0.8 mL) at a concentration of 100μg/mL in buffer (PBS containing 0.05% Tween-20) containing theneuraminidase inhibitor oseltamivir carboxylate (10 μM). The slides weregently rocked at room temperature for 90 min followed by detection withsecondary antibodies also in presence of the neuraminidase inhibitor(Table 7). TABLE 7 Valencies of Glycan Binding Proteins SecondaryTertiary Category GBP Valency Antibody Antibody^(a) Final Plant ConA-FITC 4 4 Lectin ECA-FITC 2 2 Plant Lectin Human C DC-SIGN-Fc^(b) 2 2Type Human CD22-Fc 2 α-hlgG-F^(a) α-glgG-F^(a) 8 Siglec HumanGalectin-4- 2 2 Galectin AF488 Human Anti-CD15- 2 2 IgG FITC Human 2G122 α-hlgG-F^(d) 4 IgG Human Serum^(c) 2 2 IgG/A/M BacterialCyanovirin^(d) 2 2 GBP Viral GBP Influenza HA 3 α-HA-HF^(a) α-migG- 12(H3) AF^(a) Intact Influenza 500 A-PR8 α-rlgG- 500 Virus (PR8)^(e)AF^(a)^(a)Abbreviations used: Ab = antibody; F = FITC; AF = AF488.^(b)After binding of DC-SIGN, binding was detected by overlay withanti-human IgG-AF488.^(c)After binding of serum diluted 1:25 with PBS, binding was detectedby overlay with goat anti-human IgG/M/A-Biotin (1:100) (Pierce) followedby Streptavidin-FITC (1:100).^(d)After binding of CVN, binding was detected by overlay withpolyclonal rabbit anti-CVN IgG-AF488 followed by anti-rabbit IgG-FITC.^(e)After binding of virus, binding was detected by overlay with rabbitanti-PR8 followed by goat anti-rabbit IgG-AF-488.

Image acquisition and signal processing. Fluorescence intensities weredetected using a ScanArray 5000 (Perkin Elmer, Boston, Mass.) confocalscanner and image analyses were carried out using ImaGene image analysissoftware (BioDiscovery Inc, El Segundo, Calif.). Signal to backgroundwas typically greater than 50:1 and no background subtractions wereperformed. Data were plotted using MS Excel software.

Results

Glycan array design. The strategy adopted for covalently attaching adefined glycan library to micro-glass slides employed standardmicroarray printing technology as illustrated in FIG. 1. The use of anamino-reactive NHS-activated micro-glass surface allows covalentattachment of glycans containing a terminal amine by forming an amidebond under aqueous conditions at room temperature. The compound libraryof 200 glycoconjugates comprises diverse and biologically relevantstructures representing terminal sequences of glycoprotein andglycolipid glycans. Glycan structures detected by glycan bindingproteins are listed in FIG. 2 and a more complete glycan listing isprovided in FIG. 7, Table 3 and Table 9. In addition, exemplary symbolstructures summarizing the principal specificities of each glycanbinding protein are depicted in each Figure.

Optimization of glycan printing. Length of time of the printing processwas a concern because the moisture sensitive NHS-slides would be exposedto air during the procedure. Binding of fluorescein-labeled concanavalinA (con A) was used as a measure of ligand coupling. Maximal binding ofcon A to high mannose glycans, 134-138 (structures provided in FIG. 7and Table 3), was obtained at concentrations >50 μM, with less than 10%variation in maximal binding observed with printing times up to 5 hours,as was observed for compound 136 (structure provided in FIG. 7). For thecomplete array, standard printing concentrations of 100 μM and 10 μM ofeach glycan were selected to represent saturating and sub-saturatinglevels, respectively, of the printed glycan. All samples were printed inreplicates of six to generate an array of >2400 spotted ligands perglass slide, including controls.

General approach for profiling GBP specificity. In general, GBPs havelow affinity for their ligands, and would not be expected to bind withsufficient avidity to withstand washing steps to remove unbound protein.For this reason, the approach routinely used was to create multivalencyas necessary to mimic the multivalent interactions that occur in nature.Some of the glycan binding proteins evaluated in these experiments andthe degree of multivalency used to achieve robust binding are summarizedin Table 7. The valency required for binding ranged from 2 to 12. Inseveral cases monovalent glycan binding proteins were evaluated asdivalent recombinant Ig-Fc chimeras, and in other cases, highervalencies were achieved through the use of secondary antibodies. Bindingwas detected by including a fluorescent label either on the glycanbinding protein or secondary antibody.

Specificity of plant lectins. As shown in FIG. 3, two lectins, Con A andErythrina cristagalli lectin (ECA) exhibited binding to differentsubsets of glycans on the array, consistent with their reportedspecificities. Con A bound selectively to synthetic ligands consistingof one or more α-D-mannose (Manα1) residues as well as to isolatedhigh-mannose N-glycans, and a bi-antennary N-linked glycan (134-145,199, see FIG. 7). ECA bound exclusively to various terminalN-acetyllactosamine (LacNAc) structures, poly-LacNAc (9, 73, 76, seeFIG. 7) and branched O-glycans (49, 72, see FIG. 7). ECA also toleratedterminal Fucα1-2Gal substitution (105-107, see FIG. 7). Thesespecificities are consistent with those previously observed using othermethodologies. See, e.g., Gupta et al. (1996) Eur. J. Biochem. 242,320-326; Brewer et al. (1985) Biochem. Biophys. Res. Commun. 127,1066-71; Lis et al. (1987) Meth. Enzymol. 138, 544-551; Iglesias et al.(1982) Eur. J. Biochem. 123, 247-252.

Analysis of specificities of human GBPs. Three major families ofmammalian glycan binding proteins (GBPs) are involved in cell surfacebiology through recognition of glycan ligands—C-type lectins, siglecsand galectins. One exemplary member from each class was selected foranalysis (FIG. 4).

DC-SIGN, a member of the group 2 subfamily of the C-type lectin family,is a dendritic cell protein implicated in innate immunity and thepathogenicity of human immunodeficiency virus-1 (HIV-1) (Kooyk, Y. &Geijtenbeek, T. B. (2002) Immunol. Rev. 186, 47-56). As shown in FIG. 4,a recombinant DC-SIGN-Fc recognized two classes of glycans, variousfucosylated oligosaccharides with the Fucα1-3 GlcNAc and Fucα1-4GlcNAcoligosaccharides found as terminal sequences on N-and O-linkedoligosaccharides (7, 8, 51, 66, 94, 102, see FIG. 7), and mannosecontaining oligosaccharides terminated with Manα1-2-residues (135-138,144, 145, see FIG. 7), consistent with specificities found by othergroups, for example, as described in Guo et al. (2004) Nat. Struct. MolBiol. 11, 591-8; van Die et al. (2003) Glycobiology 13, 471-478; andAdams et al. (2004) Chem.l Biol. 11, 875-81.

CD22, a member of the immunoglobulin superfamily lectins (Siglecs), is awell-known negative regulator of B cell signaling and binds selectivelyto glycans with Siaα2-6Gal-sequences. Blixt et al. (2003) J. Biol. Chem.278, 31007-19; Engel et al. (1993) J. Immunol. 150, 4719-4732; Kelm etal. (1994) Curr. Biol. 4, 965-72; Powell et al. (1993) J. Biol. Chem.268, 7019-7027. As shown in FIG. 4B, CD22 bound exclusively to the sevenstructures containing the terminal Siaα2-6Galβ1-4GlcNAc-sequenceincluding a bi-antennary N-linked glycan (154, 187-189 and 199, see FIG.7). An additional 6-O-GlcNAc-sulfation(Neu5Acα2-6Galβ1-4[6Su]GlcNAc-183, see FIG. 7) appeared to enhancebinding relative to the corresponding non-sulfated glycan, suggestingthat this glycan could be a preferred ligand for human CD22.

Galectins are a family of β-galactoside binding lectins that bindterminal and internal galactose residues. See, Hirabayashi et al. (2002)Biochim. Biophys. Acta 1572, 232-54. Galectin-4 has been identified as apossible intracellular mediator with anti-apoptotic activity. Huflejt etal. (1997) J. Biol. Chem. 272, 14294-303; Huflejt, M. E. & Leffler, H.(2004) Glycoconjugate J. 20, 247-55. By comparing Galectin-4 binding tosaturated glycans (printed at 100 μM concentration) with binding tosub-saturated glycans (printed at 10 μM concentration), preferredbinding specificities were revealed. In particular, as shown in FIG. 4C,Galα1-3-linked to lactose (35-37), Fucα1-2-linked to lac(NAc) (100, 103,105-107), or GlcNAcβ1-3-linked to lactose (123), as well as 3′-sulfation(11-16) substantially enhanced the affinity. This specificity profile issimilar to that reported for a rat ortholog of Galectin-4. See Wu et al.(2004) Biochimie 86, 317-26; Oda et al. (1993) J. of Biol. Chem. 268,5929-5939.

Glycan specific antibodies. Monoclonal and polyclonal anti-glycanantibodies from three different sources were also analyzed (FIG. 5). Thecommercial leukocyte differentiation antigen CD-15 has been documentedto recognize a carbohydrate antigen, Lewis^(x) (Galβ1-4[Fucα1-3]GlcNAc).When evaluated on the array described herein this antibody was highlyspecific for Lewis^(x) structures (7, 8, 66, see FIG. 7), and did notrecognize the same structure modified by additional sialylation (161),sulfation (26), fucosylation (102) or LacNAc extension (73)(see FIG. 7for structures). FIG. 5A shows the specificity of an anti-CD15 antibodypreparation for Lewis^(X) glycans.

One of the most studied human anti-HIV monoclonal antibodies is 2G12,which neutralizes a broad spectrum of natural HIV isolates viarecognition of high mannose type N-linked glycans on the major envelopeglycoprotein, gp120. Lee et al. (2004) Angew. Chem. Int. Ed. 43,1000-1003; Calarese et al.(2003) Science 300, 2065-71; Scanlan et al.,(2002) J. Virol. 76, 7306-21; Sanders (2002) J. Virol. 76, 7293-305;Trkola et al. (1996) J. Virol. 70, 1100-8. The glycan array contains avariety of synthetic mannose fragments with the natural series of highmannose N-glycans (Man5-Man9) isolated from ribonuclease B.

As shown in FIG. 5B, recombinant 2G12 exhibited strong binding ofsynthetic Manα1-2-terminal mannose oligosaccharides (135, 136, 138). Seealso Bryan et al. (2004) J. Am. Chem. Soc. 126, 8640-41; Lee et al.(2004) Angew. Chem. Int. Ed. 43, 1000-1003; Adams et al. (2004) Chem.lBiol. 11, 875-81. In addition, of the series of natural high mannosetype N-glycans, 2G12 exhibited preferred binding to Man8 glycans (144)relative to Man5, Man6, Man7 or Man9 glycans (140, 142, 143, 145) (seeFIG. 7 for these structures).

In particular, the glycans to which the 2G12 antibodies bound had anythe following Man-8 N-glycan structures, or were a combination thereof:

wherein each filled circle (•) represents a mannose residue.

A smaller level of binding was observed between the 2G12 antibodies andMan-9-N-glycans. As shown in Table 8, simpler synthetic glycans bind2G12 as well as the Man8 glycans. However, the simpler compounds aremore likely to elicit an immune response that will generate antibodiesto the immunogen, but not the high mannose glycans of the gp120. Thenatural structure is also less likely to produce an unwanted immuneresponse. Indeed, yeast mannan is a polymer of mannose and is a potentimmunogen in humans, representing a major barrier to production ofrecombinant therapeutic glycoproteins in yeast. TABLE 8 Summary of thebinding of 2G12 to mannose containing glycans in the glycan array shownin FIG. 7. Samples 1-6 are glycoproteins, samples 134-139 are synthetichigh mannose glycans, samples 140-145 are natural high mannoseglycopeptides isolated from bovine ribonuclease, and sample 199 is abi-antennary complex type glycan terminated in sialic acid. No. Mannosecontaining ligands Rel. spec. 1 Alpha1-acid glycoprotein − 2 Alpha1-acidglycoprotein A − 3 Alpha1-acid glycoprotein B − 4 Ceruloplasmin − 5Transferrin − 6 Fibrinogen − 134 Ma#sp3 − 135 Ma2Ma2Ma3Ma#sp3 +++ 136Ma2Ma3[Ma2Ma6]Ma#sp3 +++ 137 Ma2Ma3Ma#sp3 − 138 Ma3[Ma2Ma2Ma6]Ma#sp3 +++139 Ma3[Ma6]Ma#sp3 − 140 Man-5#aa − 142 Man-6#aa − 143 Man-7#aa − 144Man-8#aa +++ 145 Man-9#aa + 199 OS-11 −Relative binding activity:− = <1000;+ = 1000-6000;++ 6000-25,000; and+++ >25,000.

These results indicate that glycans with eight mannose residues aresuperior antigens for binding the 2G12 anti-HIV neutralizing antibodies.

To test the array against more complex samples, anti-glycan antibodiespresent in human serum and saliva were investigated. Followingincubation with serum or saliva, bound IgG, IgA and IgM were detected onthe glycan array using labeled anti-human IgG/A/M antibody.

A surprising diversity of antibody specificities was observed in bothserum and saliva. The binding results observed for serum samples fromten individuals are shown in FIG. 5C. This profile of human anti-glycanantibodies detects the ABO blood group fragments (variously representedin different individuals) (32, 81, 83), mannose fragments (135-139),α-Gal-(31-37) and ganglioside-epitopes (55-59, 132, 168), as well asfragments of the gram negative bacterial cell wall peptidoglycan (127)and rhamnose (200)(see FIG. 7 for these structures). Notably, glycanscontaining the Galβ1-3GlcNAc sub-structure were consistently detected(12, 61, 62, 132, 150, 168) except when fucosylated (25, 51, 94, 100)thus generating the human blood group antigens H, Lewis^(a) or Lewis^(b)(see FIG. 7 for structures). All of these structures can be identifiedas either blood group antigens or fragments of microorganisms (e.g.bacteria, yeast etc.) to which humans are exposed.

A variety of glycan binding proteins are also detected in saliva, asshown in FIG. 12.

Analysis of bacterial and viral GBPs. Cyanovirin-N (CVN) is acyanobacterial protein that can block the initial step of HIV-1infection by binding to high mannose groups on the envelope glycoproteingp120. Adams et al. (2004) Chem. Biol. 11, 875-81; Bewely, C. A. &Otero-Quintero, S. (2001) J. Am. Chem. Soc. 123, 3892-3902. On thearray, CVN specifically recognized the synthetic fragments bearingterminal Manα1-2-residues (135-138), as well as high mannose glycanswith one or more Manα1-2-termini (140-145), in keeping with its reportedspecificity (FIG. 6 and 7). In addition, CVN bound to several lacto- andneolacto-structures (53, 62, 75, 176, see FIG. 6 and 7).

Influenza viruses exhibit specificity in their ability to recognizesialosides as cell surface receptor determinants through the viralbinding protein, the hemagglutinin. Depending on the species of origin,the hemagglutinin has specificity for sialosides with sialic acid in theNeuAcα2-3Gal or NeuAcα2-6Gal linkage. Connor et al. (1994) Virol. 205,17-23; Rogers, G. N. & D'Souza, B. L. (1989) Virol. 173, 317-22; Rogerset al. (1983) Nature 304, 76-8. While the intrinsic affinity ofsialosides for the hemagglutinin is weak (Kd≈2 mM), binding isstrengthened through polyvalent interactions at the cell surface. Sauteret al. (1989) Biochem. 28, 8388-96.

Results shown in FIG. 6B reveal the binding of a recombinant avian H3hemagglutinin (Duck/Ukraine/1/63) bound to Neu5Acα2-3-linked togalactosides (24, 162-169, 176-180, see FIG. 7), but not to anyNeu5Acα2-6- or Neu5Acα2-8-linked sialosides. Intact influenza viruses,such as A/Puerto Rico/8/34 (H1N1), were also strongly bound to the array(FIG. 6C). The overall affinities are consistent with previous findingsand show specificity for both α2-3 and α2-6 sialosides. Rogers, G. N. &Paulson, J. C. (1983) Virol. 127, 361-73.

Detailed fine specificities were also revealed such as binding toNeu5Acα2-3- and Neu5Acα2-6-linked to galactosides (24, 151, 157,161-180, 182-190, 199, see FIG. 7), as well as certain O-linkedsialosides.

Thus, the glycan microarrays described herein can be used to detect avariety of glycan binding entities. The microarrays can be made byrobotic printing, and binding to the microarrays can be detected byscanning and image analysis software used for DNA microarrays. Thecombination of using amine-functionalized glycans with the NHS-activatedglass surface results in robust and reproducible covalent attachment ofglycans with no modifications of standard DNA printing protocols. Thearray can be used with no further preparation of the surface forassessing the specificity of a wide variety of glycan binding proteins,yielding uniformly low backgrounds regardless of the labeled proteinused for detection. Moreover, only 0.1-2 μg of glycan binding protein isneeded for optimal signal, over 100-fold less than required for an ELISAbased array that uses predominately the same glycan library. Fazio etal. (2002) J. Am. Chem. Soc. 124, 14397-14402. The arrays performed wellfor a wide variety of glycan binding proteins, confirming primaryspecificities documented by other means, and revealing novel aspects offine specificity that had not previously been recognized.

EXAMPLE 6 Diagnosis of Neoplasia using Glycan Arrays

This Example illustrates that antibodies present in breast cancerpatients can be detected using the glycan arrays of the invention. Onlya small sample volume of human serum was needed for detecting antibodiesthat bound to specific types of glycans. Thus, the invention providesnon-invasive screening procedures for detecting breast neoplasia.

Materials and Methods:

Individual (not pooled) sera were collected from 9 patients who werediagnosed with metastatic breast cancer (MBC). Blood samples werecollected before treatment, so that therapeutic intervention would notinterfere with patient immune responses. One patient with breast cancerbut with good prognosis (IDC, Stage 1) was also included in the study.As control, or “healthy” sera, sera from ten healthy individuals, 5female and 5 male, with no known malignancies was collected.

Sera were diluted 1:25 with PBS containing 3% BSA, and placed on theglycan array slide in humidified chamber at room temperature for 90 min.The glycan array slide was then rinsed gently with PBS/0.05% Tween,incubated with biotinylated goat antibody against human IgG, IgM andIgA, rinsed in PBS/0.05% Tween, and incubated with streptavidin-Alexa488fluorescent dye. Following rinses in PBS/0.05% Tween and H₂O, glycanarray slides were dried and scanned using the commercial DNA arrayscanner. The images were analyzed and intensity of fluorescence in spotscorresponding to the antibodies bound to the individual glycans wasquantified using a ScanArray 5000 (Perkin Elmer, Boston, Mass.) confocalscanner and image analyses were carried out using ImaGene image analysissoftware (BioDiscovery Inc, El Segundo, Calif.). Signal to backgroundwas typically greater 50:1 and no background subtractions wereperformed. Data were plotted using MS Excel software.

Results

The results of these experiments are provided in FIGS. 8-10. A profileof the relative fluorescence intensity of labeled antibodies bound tospecific glycans on the array is provided in FIG. 8. As illustrated inFIG. 8, there are significant differences between the reactivity of serafrom controls and from patients with metastatic breast cancer. Inparticular, the levels of certain anti-carbohydrate antibodies are muchhigher in patients with metastatic breast cancer. Glycans to which serafrom metastatic cancer patients bind include ceruloplasmin,Neu5Gc(2-6)GalNAc, GM1, Sulfo-T, Globo-H, and LNT-2.

GM1 has the following structure:Gal-beta3-GalNAc-beta4-[Neu5Ac-alpha3]-Gal-beta4-Glc-beta.

The sulfo-T antigens are T-antigens with sulfate residues. In general, Tantigens have the structure Galβ3GalNAc and can have variousmodifications. LNT-2 is a ligand for tumor-promoting Galectin-4. SeeHuflejt & Leffler (2004) Glycoconjugate J., 20: 247-255). The structureof LNT-2 includes the following glycan: GlcNAc-beta3-Gal-beta4-Glc-beta.

Globo-H has the following structure:Fucose-alpha2-Gal-beta3-GalNAc-beta3-Gal-alpha4-Gal-beta4-Glc.

The antibodies that bind to these glycans therefore react with a seriesof glycan types. The clusters of glycans reactive with these antibodiesdefine the neoplasia status more precisely then would detection of anindividual antibody alone. Moreover, the levels of the antibodiesreactive with individual glycan clusters can be quantified and convertedinto score values used for mathematical and statistical serum sampleanalysis that would allow diagnostic assignment of the neoplasia riskfor the individual patient, when compared with the value rangecharacteristic of the individuals with no known neoplasia.

Specifically, antibodies against ceruloplasmin (FIG. 8, compound no. 2)and against cancer specific carbohydrate antigenNeu5Acα2-6GalNAcα-(STn-, FIG. 8, compound no. 3 and 4) appear atsignificantly higher levels in all MBC patients as compared to “healthy”individuals. There are also antibodies against other specific glycansthat are present in metastatic breast cancer patients at the levelshigher than in the healthy individuals. These specific glycan categoriesinclude: a group of T-antigens carrying various modifications (see FIG.9, compounds no. 5, 8-13), LNT-2 (a known ligand for tumor-promotingGalectin-4, Huflejt and Leffler, 2004), Globo-H—, and GM1-antigens.

As shown in FIG. 10, combining the relative fluorescence intensitiescorresponding to the levels of serum antibodies listed in FIG. 9 foreach patient allows generation of the antibody signal range thatprovides a clear distinction between cancer and non-cancer population.There fore, this test can provide an additional tool for appropriatecorrelation between specific glycoprotein profiles and various stages ofdisease to allow for identification of appropriate therapeutic targets.

These findings suggest that more than one glycan is present as anaturally occurring epitope during malignant transformation in breastcancer patients and these epitopes elicit immune response in each of theso far examined (breast) cancer patients. Moreover, these resultsindicate that clusters of different antibodies reactive againsttumor-associated glycans can be detected simultaneously in theindividual patient sera. Such detection of several antibody typesprovides much better diagnostic information than information about thepresence of a single type of antibody reactive with a single type ofglycan.

These combined tumor-associated glycans will be the preferred immunogenfor a vaccine composition to elicit an immune response that results inproduction of antibodies neutralizing antibodies activities oftumor-promoting glycans. Such compositions will likely includemultivalent glycans to mimic the clustered N-linked glycan epitopes oncellular surfaces of cancer, stromal, and endothelial cells.

EXAMPLE 7 Antibodies Against Alpha-Gal-3 Glycan Epitopes Were Detectedin Sera of Patients Receiving Xenotransplants

This Example illustrates that several here-to-fore unidentified glycanstructures contribute to acute organ rejection after transplantation ofpig tissues into humans.

As is generally known by one of skill in the art, humans exhibit animmune response to alpha-Gal-3 glycan epitopes because these glycans areabundant on pig cell surfaces. Hence, an immune response against thesealpha-Gal-3 epitopes has been a major problem that must be overcome topermit xenotransplantation of tissues. However, as illustrated in thisExample other glycan structures contribute to acute organ rejection.These transplant-associated glycan structures are identified anddescribed in this Example.

Materials and Methods

In 1991-1994, several diabetic (I) patients received transplantation ofporcine fetal pancreas islet-like cell clusters (ICC). See, Groth, C. G.et al. Transplantation of porcine fetal pancreas to diabetic patients,The Lancet 344: 1402-4 (1994). The inventor analyzed serum from three ofthese patients before transplant (t=0), 1 months after (t=1), 6 monthsafter (t=2) and 12 months after (t=3) transplant.

Sera were diluted as needed with PBS containing 3% BSA, and placed onthe glycan array slide in humidified chamber at room temperature for 90min. The glycan array slide was then rinsed gently with PBS/0.05% Tween,incubated with biotinylated goat antibody against human IgG, IgM andIgA, rinsed in PBS/0.05% Tween, and incubated with streptavidin-Alexa488fluorescent dye. Following rinses in PBS/0.05% Tween and H₂O, glycanarray slides were dried and scanned using the commercial DNA arrayscanner. The images were analyzed and intensity of fluorescence in spotscorresponding to the antibodies bound to the individual glycans wasquantified using a ScanArray 5000 (Perkin Elmer, Boston, Mass.) confocalscanner and image analyses were carried out using ImaGene image analysissoftware (BioDiscovery Inc, El Segundo, Calif.). Signal to backgroundwas typically greater 50:1 and no background subtractions wereperformed. Data were plotted using MS Excel software.

Results

FIG. 11 provides representative results from one patient. Similarresults were seen for all patients analyzed. Glycans 33-39 (structuresshown in FIG. 7) are identified as glycans 1-7 in FIG. 11D. Whileglycans 33-39 do not have identical structures, each of them terminatewith alpha-Gal. Compared with the reactivity of serum taken at t=0(lighter, blue bars), serum taken at 1 month after (t=1), 6 months after(t=2) and 12 months after (t=3) transplantation have significantlygreater amounts of anti-glycan antibodies. Compound 8 is LeX(Gal-beta4-GlcNAc[alpha3-Fucose]-beta, structure 65 in FIG. 7) andhumans do not have antibodies to this glycan structure because it is onhuman cells. The last structure 9, is alpha-Gal-LeX(Gal-alpha3-Gal-beta4-GlcNAc[alpha3-Fucose]-beta (structure 34 in FIG.7), also shown in FIG. 11C), is not found in humans, but has beenreported to be present on porcine kidney cells. See Bouhors D. et al.,Gala1-3-LeX expressed on iso-neolacto ceramides in porcine kidneyGLYCOCONJ. J. (10) 1001-16 (1998). However, patients who receivedtransplantation of porcine fetal pancreas islet-like cell clustersclearly exhibit an immune response (antibody production) againststructure 9 (alpha-Gal-LeX).

Thus, as shown in FIG. 11, the glycan arrays and methods of theinvention for testing whether antibodies were present in serum oftransplant recipients, illustrate that distinct differences exist inantibody responses before and after receiving tissue transplantation.The arrays and methods of the invention are therefore useful formonitoring and evaluating graft rejection after transplantation and/orxenotransplantation.

Further examples of glycans that can be used in the compositions,libraries, arrays and methods of the invention are provided in Table 9.Note that a spacer or linker can be attached to the glycan either as analpha or beta linkage. In some cases, the spacer or linker is attachedto the reducing end of the glycan. TABLE 9 IUPAC Xylb Fuca Rhaa GalbGlcb Mana Alt Manb Gala Glca GlcAa GlcNAcb GlcNAca GalNAca GalNAcbMan[6P]a Man[6P]b Gal[3S]b GlcNAca[1P] GalNAc[3S]b GalNAc[6S]aGlcNAc[6S]b NeuAca NeuAcb Xylb1-2Manb Galb1-4Xylb Xyla1-3Glcb NeuGcaNeuGcb Glcb1-3Fuca Fuca1-2Galb Glcb1-3Fuca Fuca1-2Galb Gala1-4GalbGala1-6Glcb Mana1-2Mana Mana1-2Man Glca1-6Mana Mana1-6Mana Galb1-4GlcbGlcb1-4Glcb Glcb1-6Glcb Mana1-3Man Galb1-6Glcb Galb1-4Glcb Galb1-3GlcbGlca1-4Glcb Galb1-3Gal Mana1-6Mana Galb1-4Galb Galb1-4Gala Gala1-4GalbGalb1-4Glcb Galb1-4Glcb Galb1-3Galb Galb1-2Galb Gala1-3Galb Gala1-2GalbMana1-2Mana Mana1-6Mana Mana1-2Man Galb1-4Gala Glcb1-2Galb Galb1-4GlcbMana1-2Mana Glca1-6Mana Galb1-4Glcb Glca1-4Glcb Gala1-2Man Mana1-6ManGlca1-4Glcb Glca1-4Glcb Glca1-2Gal Mana1-2Mana Galb1-4GlcbFuca1-6GlcNAcb Fuca1-4GlcNAcb Fuca1-3GlcNAcb Fucb1-6GalNAc GalNAca1-3FucFuca1-6GlcNAc GlcNAcb1-2Man Galb1-3GalNAc GlcNAcb1-2Man Galb1-3GalNAcaGalNAcb1-4Glcb Gala1-3GalNAc Galb1-4GlcNAca Galb1-4GlcNAc Galb1-3GalNAcaGalb1-3GalNAca Galb1-3GlcNAc Galb1-4GlcNAc Galb1-4GlcNAcb Galb1-3GlcNAcbGalb1-3GalNAca GalNAca1-3Galb Galb1-3GalNAca Galb1-6GalNAc Gala1-4GlcNAcGalb1-4GlcNAcb Galb1-3GalNAc Galb1-4GlcNAca Galb1-4GlcNAcbGala1-3GalNAca Gala1-3GalNAca GlcNAcb1-4Man Galb1-3GalNAcaGalb1-3GalNAcb Galb1-3GalNAcb Galb1-3GlcNAcb Gala1-3GalNAcbGlcNAcb1-6Mana1-6 Manb1-4GlcNAc Galb1-3GalNAca Galb1-3GlcNAcbGalb1-4GlcNAcb Galb1-4GlcNAcb Galb1-3GlcNAca Galb1-4GlcNAcaGalb1-3GalNAcb Galb1-3GalNAcb Galb1-3GlcNAcb Galb1-4Xyl[2P]bMan[6P]a1-2Man Gal[6S]b1-4Glcb Gal[2S]b1-4Glcb Gal[2S]b1-4GlcbGal[3S]b1-4Glcb Galb1-4Glc[6S]b Gal[6S]b1-4Glc Gal[6S]b1-4GlcbGal[3S]b1-4Glcb GlcNAcb1-3GalNAc GalNAca1-3GalNAc GlcNAcb1-4GlcNAcGalNAca1-6GalNAc GlcNAcb1-6GalNAc GlcNAcb1-4GlcNAcb GalNAcb1-4GlcNAcbGalNAcb1-4GalNAca GalNAca1-3GalNAca GlcNAcb1-4GlcNAcb GalNAcb1-4GlcNAcbGlcNAcb1-6GalNAca GalNAcb1-4GlcNAcb GalNAcb1-4GlcNAc GalNAcb1-3GalNAcGalNAcb1-4GlcNAc GlcNAcb1-4GlcNAcb Xyla1-3Xyla1-3Glcb Xyla1-3Xyla1-3GlcbXyla1-3Xyla1-3Glca Gal[3S]b1-3GalNAcb Galb1-4GlcNAc[6S]bGlcNAc[6S]b1-3Gal Gal[3S]b1-3GalNAca Gal[6S]b1-3GalNAc Galb1-4GlcNAc[6S]Gal[3S]b1-4GlcNAc NeuAca2-3Galb NeuAca2-6Glcb NeuAca2-6GalbKdna1-6GaNAca NeuAca2-3Gal NeuAca2-6Gal NeuAca2-3Gal NeuAca2-6GalbNeuAca2-6Gal NeuAca2-6Galb NeuAca2-3Gala Mana1-3(Xylb1-2)ManbGalb1-3Galb1-4Xylb Mana1-6(Xylb1-2)Manb GlcAb1-4GlcNAc[6S] NeuGca2-6GalNeuGca2-3Galb NeuGca2-3Gal Gala1-3(Fuca1-2)Galb Rhaa1-3Mana1-2ManGalb1-4(Fuca1-3)Glc Fuca1-2Galb1-4Glc Gala1-3(Fuca1-2)GalbFuca1-2Galb1-4Glcb Gala1-3(Fuca1-2)Galb Fuca1-2Galb1-4GlcbGala1-3(Fuca1-2)Galb Gal[3S]b1-4Glc[6S]b GalNAc[4S]b1-4GlcNAcGlca1-6Glcb1-6Glcb Glca1-6Glcb1-6Glca Mana1-2(Mana1-6)ManaGala1-4Galb1-4Glc Gala1-4Galb1-4Glcb Galb1-6Galb1-6GlcbGlca1-4Glca1-4Glcb Glcb1-6Glcb1-6Glc Gala1-2Mana1-2ManMana1-2(Mana1-4)Mana Manb1-2Manb1-2Man Glca1-3(Mana1-2)ManMana1-3(Mana1-6)Mana Mana1-3(Mana1-6)Mana Mana1-2(Mana1-6)ManaMana1-2Mana1-2Mana Gala1-4Galb1-4Glcb Glca1-6Glcb1-6GlcbGala1-3Galb1-4Glcb Gala1-3(Mana1-2)Man Glcb1-6(Glca1-6)GlcaGala1-6Gala1-6Glcb Mana1-6Mana1-6Man Manb1-4Manb1-4ManMana1-2Mana1-2Mana Mana1-3(Mana1-6)Mana Gala1-4Galb1-4GlcbGala1-3Galb1-4Glcb Mana1-3(Mana1-6)Man Mana1-2Mana1-2Man NeuAca2-6GalNAcNeuAca2-6GlcNAcb NeuAca2-3GalNAca Fuca1-3(Fuca1-6)GlcNAcbAra'b1-3GlcNAcb1-2Man NeuGca2-6GalNAca NeuGca2-6GalNAcFuca1-2Galb1-3GalNAc Fuca1-2Galb1-3GlcNAc Fuca1-2Galb1-4GlcNAcGalb1-4(Fuca1-3)GlcNAcb Galb1-4(Fuca1-3)GlcNAc GalNAca1-3(Fuca1-2)GalbGalb1-4(Fuca1-6)GlcNAcb Fuca1-2Galb1-4GlcNAcb Fuca1-3GlcNAcb1-2ManGalb1-3(Fuca1-4)GlcNAc Galb1-3(Fuca1-4)GlcNAcb GalNAca1-3(Fuca1-2)GalGalNAca1-3(Fuca1-2)Galb Galb1-4(Fuca1-3)GlcNAcb Fuca1-2Galb1-4GlcNAcbGalb1-3(Fuca1-4)GlcNAcb Fuca1-2Galb1-3GalNAcb Fuca1-2Galb1-3GalNAcaGlcb1-4(Fuca1-6)GlcNAcb Galb1-4(Fuca1-3)GlcNAcb Fuca1-2Galb1-3GalNAcaFuca1-2Galb1-4GlcNAcb Fuca1-2Galb1-3GlcNAcb Fuca1-2Galb1-4GlcNAcbGalb1-4(Fuca1-3)GlcNAc Fuca1-2Galb1-3GlcNAcb Fuca1-2Galb1-3GlcNAcbFuca1-2Galb1-3GlcNAcb Fuca1-2Galb1-3GlcNAcb GalNAca1-3(Fuca1-2)GalbGalb1-3(Fuca1-4)GlcNAcb Galb1-3(Fuca1-4)GlcNAcb GlcNAcb1-6(GlcNb1-2)ManaGala1-3Galb1-4GlcNAcb GlcNAcb1-3Galb1-4Glc Galb1-3(Galb1-6)GalNAcGlcNAcb1-3Galb1-4Glcb Mana1-3Manb1-4GlcNAc Galb1-4Galb1-3GalNAcGala1-3Galb1-3GlcNAcb GlcNAcb1-2Mana1-3Manb GlcNAcb1-3Galb1-4GlcbGala1-4Galb1-4GlcNAcb Gala1-3Galb1-3GlcNAcb Gala1-4Galb1-4GlcNAcbGalb1-4(GlcNAcb1-2)Man Galb1-4GlcNAcb1-6Man Gala1-3Galb1-4GlcNAcGlcNAcb1-3Galb1-4Glcb Galb1-3Galb1-3GalNAc GlcNAcb1-6Mana1-6ManMana1-6Manb1-4GlcNAc Gala1-3Galb1-4GalNAc Galb1-3(Galb1-6)GlcNAcGala1-3Galb1-4GlcNAc Mana1-3Manb1-4GlcNAc Galb1-3GlcNAcb1-3GalGlcNAcb1-6Mana1-6Manb Galb1-4GlcNAcb1-3Gal Galb1-4Galb1-3GalNAcaGalb1-4GlcNAcb1-2Mana Galb1-4(Galb1-6)GlcNAc Galb1-4GlcNAcb1-2ManNeuAc[8S]a1-6Glcb Galb1-3Galb1-4Xyl[2P]a Galb1-3(Neua1-6)GalNAcGlcAb1-3Galb1-3GalNAc Neua1-3Galb1-3GalNAc GlcNAcb1-4(Fuca1-6)GlcNAcGalNAcb1-4(Fuca1-3)GlcNAc GalNAcb1-4(Fuca1-3)GlcNAcbGlcNAcb1-4(Fuca1-3)GlcNAcb GlcNAcb1-4(Fuca1-6)GlcNAcbMan[6P]a1-6Mana1-6Man Manb1-4GlcNAcb1-4GlcNAc Galb1-3(GlcNAcb1-6)GalNAcManb1-4GlcNAcb1-4GlcNAcb Galb1-4GlcNAcb1-3GalNAc GlcNAcb1-3Galb1-3GalNAcGalb1-3GlcNAcb1-3GalNAc Galb1-4GlcNAcb1-6GalNAc GlcNAcb1-3GalNAcb1-4GlcbManb1-4GlcNAcb1-4GlcNAc Galb1-3(GlcNAcb1-6)GalNAcaGalb1-3(GlcNAcb1-6)GalNAca Galb1-4GlcNAcb1-6GalNAcaGlcNAcb1-2(GlcNAcb1-6)Man GlcNAcb1-3Galb1-4GlcNAcbGalb1-3(GlcNAcb1-6)GalNAca GlcNAcb1-2Galb1-3GalNAcaGlcNAcb1-3Galb1-4GlcNAcb GlcNAcb1-3Galb1-4GlcNAcbGlcNAcb1-3Galb1-4GlcNAcb Galb1-4GlcNAcb1-3GalNAcaGalb1-3GlcNAcb1-6GalNAc GlcNAcb1-2(GlcNAcb1-4)ManMana1-6GlcNAcb1-4GlcNAcb Galb1-3(GlcNAcb1-6)GalNAcaGlcNAca1-4Galb1-3GalNAc GalNAca1-4Galb1-3GalNAc NeuAca2-3Galb1-4XylbFuca1-4(Gal[3S]b1-3)GlcNAcb Fuca1-3(Gal[3S]b1-4)GlcNAcbGalb1-4GlcNAc[6S]b1-3Gal Gal[3S]b1-4Galb1-3GalNAcGalNAc[3S]b1-4Galb1-4Glcb GlcNAcb1-3(GlcNAcb1-6)GalNAcGlcNAcb1-4GlcNAcb1-4GlcNAcb GlcNAcb1-6(GalNAcb1-3)GalNAcGalNAcb1-4GlcNAcb1-3GalNAc GlcNAcb1-3GalNAca1-6GalNAcGlcNAcb1-3(GlcNAcb1-6)GalNAca GlcNAcb1-3(GlcNAcb1-6)GalNAcaKdna2-3Galb1-4GlcNAcb NeuAca2-3Galb1-4Glcb Kdna1-3Galb1-4GlcNAcbKdna1-3Galb1-3GlcNAcb Kdna2-3Galb1-3GlcNAcb NeuAca2-3Galb1-4GlcbNeuAca2-6Galb1-4Glcb Kdna1-3Galb1-4GlcNAcb NeuAca2-6Galb1-4GlcbNeuAca2-3Galb1-4Glcb NeuAca2-6Galb1-4Glcb NeuAca2-3Galb1-4GlcbKdna1-3Galb1-4GlcNAcb NeuAca2-6Galb1-4Glc NeuAca2-3Galb1-4GlcFuca1-2Galb1-3(Fuca1-2)Gal Fuca1-2Galb1-4(Fuca1-3)GlcFuca1-2Galb1-4(Fuca1-2)Glcb Mana1-3(Mana1-6)(Xylb1-2)ManbNeuGca2-3Galb1-4Glcb NeuGca2-3Galb1-4Glcb NeuGca2-3Galb1-4GlcbGlcAb1-3Galb1-3Galb1-4Xylb Gala1-3(Fuca1-2)Galb1-4GlcbGalb1-4(Fuca1-3)Glcb1-3Galb Gala1-3(Fuca1-2)Galb1-4GlcbGala1-3(Fuca1-2)Galb1-4Glc Rhaa1-4GlcAa1-2Mana1-2ManGalNAc[4S]b1-4GlcNAcb1-2Man GlcNAc[6S]b1-3Galb1-3GalNAcGalb1-4GlcNAc[6S]b1-3GalNAc Gal[3S]b1-4GlcNAcb1-6GalNAcaGal[6S]b1-4GlcNAcb1-3GalNAc Gal[6S]b1-3GlcNAcb1-3GalNAcGalb1-3Gala1-4Galb1-4Glcb Gala1-2Gala1-2Mana1-2ManMana1-3Mana1-2Mana1-2Mana Glca1-2Glca1-3Glca1-3ManMana1-3Mana1-2Mana1-2Mana Mana1-3Mana1-2Mana1-2ManMana1-3Mana1-3Mana1-2Mana Glcb1-6Glcb1-6Glcb1-6GlcGala1-3Gala1-4Galb1-4Glcb Gala1-2(Gala1-6)Gala1-4ManGala1-2Gala1-6Gala1-4Man NeuAca2-3Galb1-4GlcNAcb NeuAca2-3Galb1-3GalNAcNeuAca2-3Galb1-3GalNAca Galb1-3(NeuAca2-6)GalNAc NeuAca2-3Galb1-3GalNAcaGalb1-3(NeuAca2-6)GalNAca Galb1-3(NeuAca2-6)GalNAcaNeuAca2-3Galb1-3GlcNAc NeuAca2-3Galb1-4GlcNAc NeuAca2-3/6Galb1-3GalNAcaNeuAca2-3Galb1-3GalNAca NeuAca2-6Galb1-4GlcNAcb NeuAca2-3Galb1-3/4GlcNAcNeuAca2-6Galb1-4GlcNAc NeuAca2-6Manb1-4GlcNAc NeuAca2-3Galb1-4GlcNAcNeuAca2-3Galb1-3GalNAca Galb1-3(NeuAca2-6)GlcNAcGalb1-3(NeuAca2-6)GalNAc NeuAca2-3Galb1-3GalNAcGalb1-3(NeuAca2-6)GalNAca Galb1-3(NeuAca2-6)GalNAcaNeuAca2-3Galb1-3GlcNAcb NeuAca2-3Galb1-3GlcNAcb NeuAca2-3Galb1-3GalNAcaNeuAca2-6Manb1-4GlcNAc Galb1-3(NeuAca2-6)GalNAca NeuAca2-3Gala1-4GlcNAcbNeuAca2-6Galb1-3GalNAca6 NeuAca2-3Galb1-3GlcNAcb NeuAca2-3Galb1-4GalNAcGalb1-3(NeuAca2-6)GalNAcb NeuAca2-3Galb1-3GlcNAcbNeuAca2-3Galb1-4GlcNAcb NeuAca2-3Galb1-3GlcNAcb NeuAca2-3Galb1-3GlcNAcGalb1-3(NeuAca2-6)GalNAca NeuAca2-3Gala1-3GlcNAcbNeuAca2-3Galb1-4GlcNAcb NeuAca2-3Galb1-3GalNAca NeuAca2-3Galb1-3GalNAcaNeuAca2-3Galb1-3GalNAc Galb1-3(NeuAcb2-6)GalNAca NeuAca2-6Galb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb NeuAca2-3Galb1-4GlcNAcb NeuAca2-3Galb1-3GalNAcaGalb1-3(NeuAca2-6)GalNAca NeuAca2-3Galb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb NeuAca2-3Galb1-4GlcNAc NeuAca2-3Galb1-3GalNAcaNeuAca2-6Galb1-3GalNAca NeuAca2-6Galb1-4GlcNAcb NeuAca2-6Galb1-3GalNAcaNeuAca2-3Galb1-3GalNAcb Fuca1-2Galb1-4(Fuca1-3)GlcNAcbFuca1-2Galb1-4(Fuca1-3)GlcNAcb Fuca1-2Galb1-3(Fuca1-4)GlcNAcbFuca1-2Galb1-4(Fuca1-3)GlcNAcb Fuca1-2Galb1-3(Fuca1-2)GalNAcFuca1-2Galb1-4(Fuca1-3)GlcNAc Fuca1-2Galb1-3(Fuca1-4)GlcNAcNeuGca2-3Galb1-3GalNAc Galb1-3(NeuGca2-6)GalNAc NeuGca2-6Galb1-4GlcNAcbNeuGca2-3Galb1-4GlcNAcb NeuGca2-3Galb1-4GlcNAcb NeuGca2-6Galb1-4GlcNAcbNeuGca2-3Galb1-3GlcNAcb NeuGca2-6Galb1-4GlcNAcb NeuGca2-3Galb1-4GlcNAcbNeuGca2-6Galb1-4GlcNAcb NeuGca2-3Galb1-4GlcNAcbGalb1-4(Fuca1-3)GlcNAcb1-2Man Gala1-3(Fuca1-2)Galb1-4GlcNAcbGalNAca1-3(Fuca1-2)Galb1-4Glcb Gala1-3(Fuca1-2)Galb1-3GalNAcaGala1-3(Fuca1-2)Galb1-4GlcNAcb Gala1-3Galb1-4(Fuca1-2)GlcNAcbGala1-3Galb1-4(Fuca1-3)GlcNAcb Gala1-3Galb1-3(Fuca1-2)GlcNAcbGalNAca1-3(Fuca1-2)Galb1-4Glcb Gala1-3Galb1-4(Fuca1-3)GlcNAcbGala1-3Galb1-4(Fuca1-3)GlcNAcb Galb1-3Galb1-4(Fuca1-2)GlcNAcbGala1-3(Fuca1-2)Galb1-4GlcNAcb Gala1-3(Fuca1-2)Galb1-3GalNAcaGala1-3Galb1-3(Fuca1-2)GlcNAcb Gala1-3Galb1-4(Fuca1-3)GlcNAcGala1-4(Fuca1-2)Galb1-3GalNAc Fuca1-2Galb1-3(Galb1-6)GalNAcGalNAca1-3(Fuca1-2)Galb1-4Glcb Mana1-3(Mana1-6)Manb1-4GlcNAcMana1-2Mana1-3Manb1-4GlcNAc Mana1-3Mana1-6Manb1-4GlcNAcGalNAcb1-3Gala1-4Galb1-4Glc GalNAcb1-4Gala1-4Galb1-4GlcbMana1-6Mana1-6Manb1-4GlcNAc GlcNAcb1-3Gala1-4Galb1-4GlcbGalb1-3GlcNAcb1-3Galb1-4Glcb Galb1-4(Galb1-2Galb1-6)GlcNAcGalb1-3(Galb1-2Galb1-6)GlcNAc GalNAcb1-3Gala1-4Galb1-4GlcbGalb1-3GlcNAcb1-3Galb1-4Glc Mana1-3(Mana1-6)Manb1-4GlcNAcGalb1-4GalNAcb1-4Galb1-4Glcb Galb1-4GlcNAcb1-3Galb1-4GlcbMana1-3Mana1-6Manb1-4GlcNAc GlcNAcb1-4(Mana1-3)(Mana1-6)ManGalb1-4GlcNAcb1-3Galb1-4Glcb Galb1-4GlcNAcb1-3Galb1-4GlcbMana1-3(Mana1-6)Talb1-4GlcNAc Galb1-3GlcNAcb1-3Galb1-4GlcbMana1-6Mana1-6Manb1-4GlcNAc Mana1-3(Mana1-6)Manb1-4GlcNAcGalb1-3GlcNAcb1-3Galb1-4Glc Galb1-3(Gala1-3Galb1-6)GalNAcGalb1-4GlcNAcb1-3Galb1-4Glc GlcNAcb1-3(NeuAca2-6)GalNAcNeuAca2-3GalNAcb1-4GlcNAc GalNAca1-3(NeuAca2-6)GalNAcNeuAca2-3GalNAcb1-4GlcNAc GalNAcb1-3(NeuAca2-6)GalNAcNeuAca2-6GalNAcb1-4GlcNAc GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAcbXylb1-2Manb1-4GlcNAcb1-4GlcNAc Kdna1-3(Kdna1-6)GalNAcaGlcAb1-3Galb1-3Galb1-4Xyl[2P]b GlcAb1-3Gal[4S]b1-3Galb1-4XylbGlcA[3S]b1-3Galb1-3Galb1-4Xyl GalNAcb1-3(NeuGca2-6)GalNAcGlcNAcb1-3(NeuGca2-6)GalNAc GalNAca1-3(NeuGca2-6)GalNAcFuca1-2Galb1-3GalNAcb1-4GlcNAc GalNAca1-3(Fuca1-2)Galb1-3GalNAcaGalNAca1-3Galb1-4(Fuca1-2)GlcNAcb GalNAca1-3(Fuca1-2)Galb1-4GlcNAcbFuca1-2Galb1-4GlcNAcb1-3GalNAc Fuca1-2Galb1-3(GlcNAcb1-6)GalNAcGalNAca1-3(Fuca1-2)Galb1-3GalNAc Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-3GalNAc GalNAca1-3Galb1-3(Fuca1-2)GlcNAcbGalNAca1-3(Fuca1-2)Galb1-3GalNAca GalNAca1-3(Fuca1-2)Galb1-4GlcNAcbGalNAcb1-3Galb1-3(Fuca1-2)GlcNAcb Fuca1-2Galb1-4GlcNAcb1-6GalNAcGalNAcb1-3Galb1-4(Fuca1-2)GlcNAcb GalNAca1-3(Fuca1-2)Galb1-4GlcNAcbManb1-4GlcNAcb1-4(Fuca1-3)GlcNAc Fuca1-2Galb1-3GlcNAcb1-3GalNAcGalb1-3(Fuca1-4GlcNAcb1-6)GalNAc Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcManb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcbGlcNAca1-3GalNAca1-3(Fuca1-2)Gal Mana1-6Manb1-4GlcNAcb1-4GlcNAcGalNAca1-3GalNAcb1-3Gala1-4Glcb Mana1-6Manb1-4GlcNAcb1-4GlcNAcbMana1-6Manb1-4GlcNAcb1-4GlcNAc Mana1-3Manb1-4GlcNAcb1-4GlcNAcGalb1-3(Galb1-4GlcNacb1-6)GalNac GalNAca1-3GalNAcb1-3Gala1-4GalbManb1-3Manb1-4GlcNAcb1-4GlcNAc Galb1-3(Galb1-3/4GlcNAcb1-6)GalNAcGalb1-4GlcNAcb1-3Galb1-3GalNAc GlcNAcb1-4Mana1-3Manb1-4GlcNAcGalb1-4GlcNAcb1-6Galb1-3GalNAc GlcNAcb1-2Mana1-6Manb1-4GlcNAcGlcNAcb1-2Mana1-3Manb1-4GlcNAc GalNAcb1-3Galb1-4Galb1-3GalNAcGalNAcb1-3Galb1-4Galb1-3GalNAca Galb1-3(Galb1-4GlcNAcb1-6)GalNAcaGlcNAcb1-4Mana1-6Manb1-4GlcNAc Mana1-3Manb1-4GlcNAcb1-4GlcNAcbGalb1-3(Galb1-4GlcNAcb1-6)GlcNAc Galb1-4GlcNAcb1-3Galb1-4GlcNAcbGalb1-4GlcNAcb1-3Galb1-4GlcNAcb Mana1-3Manb1-4GlcNAcb1-4GlcNAcGalb1-3(Galb1-4GlcNAcb1-6)GalNAca Galb1-3(Galb1-4GlcNAcb1-6)GalNAcaGlcNAcb1-6Mana1-6Manb1-4GlcNAc Galb1-3(Galb1-4GlcNAcb1-6)GalNAcaGalb1-4GlcNAcb1-3Galb1-4GlcNAcb Galb1-3(Galb1-4GalNAcb1-6)GalNAcGalb1-3GalNAca1-4Galb1-3GalNAc Galb1-3Galb1-3(GlcNAcb1-6)GalNAcManb1-4GlcNAcb1-4Manb1-4GlcNAc Galb1-4(GlcNAcb1-2)(GlcNAcb1-6)ManGalb1-3(Galb1-4GlcNAcb1-6)GalNAc Galb1-3(Galb1-3GlcNAcb1-6)GalNAcGalb1-4GlcNAcb1-3Galb1-4GlcNAcb NeuAca2-6(Gal[6S]b1-3)GalNAcaNeuAca2-3Galb1-3GalNAc[6S]a GlcAb1-3Galb1-3(GlcNAcb1-6)GalNAcNeuAca2-8NeuAca2-6Glcb Fuca1-2(Gal[3S]b1-4)Galb1-3GalNAcGalNAcb1-4(Fuca1-3)GlcNAcb1-3GalNAc Fuca1-2Gala1-3(Kdna1-6)GalNAcGala1-3(Fuca1-4Kdna1-6)GalNAc Man[6P]a1-6Mana1-6Manb1-4GlcNAcGlcNAcb1-3/4Galb1-3(GlcNAcb1-6)GalNAcGlcNAca1-4Galb1-3(GlcNAcb1-6)GalNAcGlcNAcb1-3/4/2Galb1-6/3(GlcNAcb1-3/6)GalNAcGalNAcb1-3GlcNAcb1-3Galb1-3GalNAc GlcNAcb1-3Galb1-4GlcNAcb1-3GalNAcGlcNAcb1-3(Galb1-4GlcNAcb1-6)GalNAc GlcNAcb1-3(GlcNAcb1-6)Galb1-3GalNAcaGlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-6)ManGalb1-3(GlcNAcb1-3GlcNAcb1-6)GalNAc GlcNAcb1-3Galb1-3GlcNAcb1-3GalNAcGlcNAca1-3Galb1-3GlcNAcb1-3GalNAc GlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-6)ManaGlcNAcb1-3(GlcNAcb1-6)Galb1-3GalNAc GlcNAcb1-4Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-3Galb1-4GlcNAcb1-6GalNAc Gala1-4(Fuca1-2)Galb1-3(Fuca1-2)GalNeuAca2-3(NeuAca2-6)GalNAca Rhaa1-2(Rhaa1-4)GlcAa1-2Mana1-2ManFuca1-2Galb1-3(GlcNAc[6S]b1-6)GalNAc Fuca1-2Galb1-3(NeuAca2-6)GalNAcNeuAca2-6Galb1-4GlcNAcb1-3Fuca Fuca1-2Galb1-3(NeuAca2-6)GlcNAcNeuAca2-3Galb1-4(Fuca1-3)GlcNAcb NeuAca2-6Galb1-4GlcNAcb1-3FucaNeuAca2-3(Fuca1-4)Galb1-3GlcNAcb NeuAca2-3Galb1-4(Fuca1-3)GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-3Fuca NeuAca2-3Galb1-4(Fuca1-3)GlcNAcNeuAca2-3Galb1-4(Fuca1-4)GlcNAcb NeuAca2-3Galb1-4(Fuca1-3)GlcNAcbFuca1-2Galb1-3(NeuAca2-6)GalNAca NeuAca2-6Galb1-4GlcNAcb1-3FucNeuAca2-3Galb1-3(Fuca1-4)GlcNAcb NeuAca2-3Galb1-4(Fuca1-3)GlcNAcbManb1-4GlcNAcb1-4GlcNAcaAll[P] Galb1-3(Galb1-4GlcNAc[6S]b1-6)GalNAcGal[6S]b1-4GlcNAcb1-3Galb1-3GalNAc Galb1-3(Gal[3S]b1-4GlcNAcb1-6)GalNAcGalb1-4GlcNAc[6S]b1-3Galb1-3GalNAc Mana1-3(Mana1-3(Mana1-6)Mana1-6)ManGala1-3Gala1-3Gala1-4Galb1-4Glcb Glca1-4(Glca1-4Glca1-6)Glca1-4GlcbMana1-2Mana1-3(Mana1-2Mana1-6)Man Mana1-3Mana1-3Mana1-2Mana1-2ManaMana1-2Mana1-3(Mana1-2Mana1-6)Mana Galb1-4Glcb1-2(Galb1-4Glcb1-6)ManGlcNAcb1-4GlcNAcb1-4GlcNAcb1-4GlcNAcb NeuGca2-8NeuGca2-6GalNAcFuca1-2Galb1-3(NeuGca2-6)GalNAc NeuGca2-3Galb1-4(Fuca1-3)GlcNAcbNeuGca2-3Galb1-3(Fuca1-4)GlcNAcb NeuAca2-3Galb1-4GlcNAcb1-2ManaGalNAcb1-4(NeuAca2-3)Galb1-4Glcb GlcNAcb1-4(NeuAca2-4)Galb1-4GlcbGalNAcb1-4(NeuAca2-3)Galb1-4Glcb GalNAcb1-4(NeuAca2-3)Galb1-4GlcbGlcNAcb1-4(NeuAca2-3)Gala1-4Glcb GalNAcb1-4(NeuAca2-3)Galb1-4GlcbGalNAcb1-4(NeuAca2-3)Galb1-4Glcb NeuAca2-6Galb1-6Galb1-3GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-4Man NeuAca2-6Galb1-4GlcNAcb1-3GalNeuAca2-3Galb1-4GlcNAcb1-3Gal NeuAca2-3Galb1-4GlcNAcb1-2ManFuca1-2Galb1-3(Fuca1-2)Galb1-3GalNAcGalNAca1-3(Fuca1-2)Galb1-3(Fuca1-2)GalGalb1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcbGala1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcbMana1-3(Mana1-6)(Xylb1-2)Manb1-4GlcNAcMana1-3(Mana1-6)(Xylb1-2)Manb1-4ManNAcMana1-3(Mana1-6)(Xylb1-2)Manb1-4ManNAcbMana1-3(Mana1-6)(Xylb1-2)Manb1-4GlcNAcb NeuAc[8S]a2-8NeuAca2-6GlcbGalNAcb1-4(NeuGca2-3)Galb1-4Glcb Galb1-4Galb1-3(NeuGca2-6)GalNAcFuca1-2Galb1-3GlcNAcb1-3Galb1-4Glcb Galb1-3(Fuca1-4)GlcNAcb1-3Galb1-4GlcGalb1-4(Fuca1-3)GlcNAcb1-3Galb1-4GlcXylb1-2Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcbXylb1-2Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcXylb1-2Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcGalb1-3(GalNAc[4S]b1-4GlcNAcb1-6)GalNAcaMana1-3(Mana1-6Mana1-6)Manb1-4GlcNAcMana1-3(Mana1-3Mana1-6)Manb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3Manb1-4GlcbGala1-3Galb1-4GlcNAcb1-3Galb1-4Glcb Mana1-2Mana1-2Mana1-3Manb1-4GlcNAcMana1-3(Mana1-6)Mana1-6Manb1-4GlcNAcMana1-3(Mana1-6Mana1-6)Manb1-4GlcNAcMana1-3(Mana1-3Mana1-6)Manb1-4GlcNAcMana1-2Mana1-3(Mana1-6)Manb1-4GlcNAcMana1-3(Mana1-6)Mana1-6Manb1-4GlcNAcMana1-3(Mana1-3Manb1-6)Manb1-4GlcNAc GalNAcb1-3Gala1-3Gala1-4Galb1-4GlcbGalNAcb1-4(NeuAca2-3)Galb1-3GalNAc GalNAca1-4Galb1-3(NeuAca2-6)GalNAcGlcNAca1-4Galb1-3(NeuAca2-6)GalNAc GlcNAcb1-3Galb1-3(NeuAca2-6)GalNAcNeuAca2-3Galb1-3(GlcNAcb1-6)GalNAc Galb1-3GlcNAcb1-3(NeuAca2-6)GalNAcGalb1-4GlcNAcb1-3(NeuAca2-6)GalNAc GalNAcb1-4(NeuAca2-3)Galb1-4GlcNAcNeuAca2-3Galb1-3(GlcNAcb1-4)GalNAca NeuAca2-3GalNAcb1-4GlcNAcb1-2ManGlcNAcb1-3Galb1-3(NeuAca2-6)GalNAca GalNAca1-4(NeuAca2-3)Galb1-3GalNAcNeuAca2-3Galb1-3(GlcNAcb1-6)GalNAca GalNAcb1-4(NeuAca2-3)Galb1-4GlcNAcbNeuAca2-6Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(NeuAca2-3)Galb1-4GlcNAcbGalNAcb1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcbGalNAca1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcbFuca1-2Galb1-4(Fuca1-3)GlcNAcb1-6GalNAcFuca1-3GalNAcb1-4(Fuca1-3)GlcNAcb1-4GlcbManb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAcbFuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3GalNAcManb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAcMana1-6(Xylb1-2)Manb1-4GlcNAcb1-4GlcNAcMana1-6(Xylb1-2)Manb1-4GlcNAcb1-4GlcNAcb NeuAca2-8NeuAca2-8NeuAca6Galb1-4GlcNAcb1-3(NeuGca2-6)GalNAc 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NeuGca2-3Galb1-4GlcNAc[6S]b1-3GalGalNAca1-3(Fuca1-2)Galb1-3(GlcNAcb1-6)GalNAcGlcNAca1-3GalNAca1-3(Fuca1-2)Galb1-3GalNAcGlcNAcb1-3(Galb1-4(Fuca1-3)GlcNAcb1-6)GalNAcGlcNAcb1-6Galb1-3(Fuca1-4GlcNAcb1-6)GalNAcGlcNAcb1-3(Fuca1-2Galb1-4GlcNAcb1-6)GalNAcGlcNAcb1-3Galb1-3(Fuca1-4GlcNAcb1-6)GalNAcGalb1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-6)GalNAcGlcNAca1-4(GlcNAca1-4GlcAa1-2)GlcAa1-2GalGlcA[3S]b1-4GlcA[3S]b1-4GlcA[3S]b1-4GlcbGalNAcb1-4GalNAcb1-3Galb1-4Galb1-3GalNAcGalb1-3GlcNAcb1-3(Galb1-4GlcNAcb1-6)GalNAcGlcNAcb1-3Galb1-3(Galb1-4GlcNAcb1-6)GalNAcGalb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3GalNAcGalb1-3GlcNAcb1-3Galb1-4GlcNAcb1-3GalNAcGlcNAcb1-6Galb1-3(Galb1-4GlcNAcb1-6)GalNAcGalb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)GalNAcGlcNAcb1-2Mana1-3(GlcNAc)Manb1-4GlcNAcGlcNAcb1-2Mana1-3Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-4(Mana1-3)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-2Mana1-3Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcbGalb1-3(GlcNAca1-4Galb1-4GlcNAcb1-6)GalNAcGalb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)GalNAcaGlcNAcb1-2(GlcNAcb1-6)Mana1-6Manb1-4GlcNAcGlcNAcb1-2(GlcNAcb1-6)Manb1-6Manb1-4GlcNAcGlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-3GalNAcMana1-6Manb1-4GlcNAcb1-4GlcNAcb1-4GlcNAcManb1-4GlcNAcb1-4Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)GalNAcaGalb1-3GlcNAcb1-3Galb1-3GlcNAcb1-3GalNAc NeuGca2-6Glca2-8NeuGca2-6GlcbNeuAca2-6Galb1-3(GlcNAc[6S]b1-6)GalNAcaNeuAca2-3Galb1-4GlcNAc[6S]b1-3GalNAc NeuAca2-3Galb1-3(NeuAca2-6)GalNAcaNeuAca2-3Galb1-3(NeuAca2-6)GalNAca NeuAca2-3Galb1-3(NeuAca2-6)GalNAcaNeuAca2-9NeuAca2-3Galb1-3GlcNAcb NeuAca2-3Galb1-3(NeuAca2-6)GalNAcNeuAca2-8NeuAca2-3Galb1-4GlcNAcbGlcAb1-3Galb1-3(GlcNAcb1-3GlcNAcb1-6)GalNAcNeuAca2-2Galb1-3(NeuAca2-6)GalNAc NeuAca2-3(NeuAca2-6)Galb1-3GalNAcNeuAca2-3Galb1-3(NeuAca2-6)GalNAca NeuAca2-3Galb1-3(NeuAca2-6)GalNAcNeuAca2-3(NeuAca2-6)Galb1-3GalNAc NeuAca2-3Galb1-3(NeuAca2-6)GalNAcNeuAca2-3Galb1-3(NeuAca2-6)GalNAca NeuAca2-3Galb1-3(NeuAca2-6)GalNAcaNeuAca2-3Galb1-3(NeuAca2-6)GalNAca NeuAca2-3Galb1-3(NeuAca2-6)GalNAcGlcNAcb1-3(Fuca1-3Fuca1-4Kdna1-6)GalNAcNeuGca2-3Galb1-4GlcNAc[6S]b1-3GalNAcFuca1-2Galb1-3(Gal[3S]b1-4GlcNAcb1-6)GalNAcGalNAcb1-4(GalNAca1-2Fuca1-3)GlcNAcb1-3GalNAcNeuAca2-3Galb1-3(NeuGca2-6)GalNAcb NeuGca2-3Galb1-3(NeuAca2-6)GalNAcbNeuAca2-3Galb1-3(NeuGca2-6)GalNAc 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6)GalNAcNeuAca2-3Galb1-3(Galb1-4GlcNAcb1-6)GalNAcNeuAca2-3Galb1-3(Galb1-4GalNAcb1-6)GalNAcGalb1-3GalNAca1-4Galb1-3(NeuAca2-6)GalNAcNeuAca2-3Galb1-3GalNAca1-4Galb1-3GalNAcGalNAcb1-3Galb1-4Galb1-3(NeuAca2-6)GalNAcNeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcbFuca1-2Galb1-4GlcNAcb1-3(NeuGca2-6)GalNAcNeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-4Galb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-3Galb1-4GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-4Galb1-4GlcNAcbGalb1-4GlcNAcb1-4(NeuAca2-3)Galb1-4GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-3Galb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-4Galb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-4Galb1-4GlcNAcbNeuAca2-3Galb1-3(Galb1-4GlcNAcb1-6)GalNAca1NeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcbGalb1-3(NeuAca2-3Galb1-4GlcNAcb1-6)GalNAca1NeuAca2-3Galb1-3(Galb1-4GlcNAcb1-6)GlcNAcaNeuAca2-3Galb1-4GlcNAcb1-3Galb1-3GalNAcNeuAca2-3Galb1-3(Galb1-3/4GlcNAcb1-6)GalNAcNeuAca2-3Galb1-3GlcNAcb1-3Galb1-3GalNAcGalb1-3(NeuAca2-3Galb1-4GlcNAcb1-6)GalNAcNeuAca2-6Galb1-4GlcNAcb1-3Galb1-3GalNAcNeuAca2-6Galb1-4GlcNAcb1-3Galb1-4GlcNAcbGalNAcb1-4(NeuAca2-3)Galb1-4GlcNAcb1-3GalGalb1-4GlcNAcb1-3Galb1-3(NeuAca2-6)GalNAcMana1-6Manb1-4GlcNAcb1-4(Fuca1-3)(Fuca1- 6)GlcNAcbFuca1-2Galb1-3(Galb1-4(Fuca1-3)GlcNAcb1-Fuca1-2Galb1-3(Fuca1-2Galb1-4GlcNAcb1- 6)GalNAc 6)GalNAcFuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1- 3GalNAc 3)GlcNAcMana1-3Manb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-Fuca1-2Galb1-3(Fuca1-2)Galb1-3(GlcNAcb1- 6)GlcNAcb 6)GalNAcMana1-6Manb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-Fuca1-2Galb1-3(Fuca1-2Galb1-3GlcNAcb1- 6)GlcNAc 6)GalNAcGalb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1- 3)GlcNAcb 3)GlcNAcbMana1-3(Mana1-6)(Xylb1-2)Manb1-4GlcNAcb1-Mana1-3(Mana1-6)(Xylb1-2)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcbNeuAca2-8NeuAca2-8NeuAca2-6Glcb NeuGca2-3Galb1-4GlcNAcb1-3Galb1-3GalNAcGalb1-4GlcNAcb1-3Galb1-3(NeuGca2-6)GalNAcGalNAcb1-3Galb1-4Galb1-3(NeuGca2-6)GalNAcGalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3Galb1-Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4Glcb 6)GlcNAcbMana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 3)GlcNAcbMana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-GalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-3Galb1- 3)GlcNAc 4GlcbGalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3Galb1-Galb1-4(Fuca1-3)GlcNAcb1-4Mana1-3Manb1- 4Glc 4GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-4Mana1-6Manb1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6Manb1- 4GlcNAc 4GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3Manb1-Galb1-3(Gala1-3(Fuca1-2)Galb1-4GlcNAcb1- 4GlcNAc 6)GalNAcMana1-3Mana1-6Manb1-4GlcNAcb1-4(Fuca1-Mana1-3(Mana1-2Mana1-6)Mana1-4GlcNAcb1- 3)GlcNAc 4GlcNAcMana1-3(Mana1-3Mana1-6)Manb1-4GlcNAcb1-Mana1-2Mana1-2Mana1-3Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcMana1-3(Mana1-3Mana1-6)Manb1-4GlcNAcb1-Mana1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcbMana1-3(Mana1-6)Mana1-6Manb1-4GlcNAcb1-Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Mana1- 4GlcNAcb 2ManMana1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-Mana1-2Mana1-6Mana1-6Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcMana1-6Mana1-3(Mana1-6)Manb1-4GlcNAcb1-Galb1-4(Galb1-4GlcNAcb1-3)(Galb1-4GlcNAcb1- 4GlcNAc 6)Glcb1-1Mana1-2Mana1-2Mana1-3Manb1-4GlcNAcb1-Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-4Glc 4GlcNAcbGalb1-6Galb1-4GlcNAcb1-2Mana1-6Manb1-4GlcNAcGlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1- 6)Manb1-4Galb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-Mana1-3(Mana1-6Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcMana1-3(Mana1-6Mana1-6)Manb1-4GlcNAcb1-Galb1-3GlcNAcb1-3Galb1-3GlcNAcb1-3Galb1-4Glcb 4GlcNAcbMana1-3(Mana1-6)Mana1-6Manb1-4GlcNAcb1-Mana1-2Mana1-3Mana1-6Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcMana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-Galb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1- 4GlcNAc 4GlcNAcFuca1-2Galb1-3(Fuca1-2)(Gal[3S]b1-4)Galb1-GlcNAcb1-3(NeuAca2-3Galb1-4GlcNAcb1-6)GalNAc 3GalNAcFuca1-4GlcNAcb1-3Galb1-3(Fuca1-4GlcNAcb1-Fuca1-4GlcNAcb1-6Galb1-3(Fuca1-4GlcNAcb1- 6)GalNAc 6)GalNAcGlcNAcb1-3(Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-Neua1-3Galb1-4GlcNAcb1-2Mana1-3Manb1- 6)GalNAc 4GlcNAcGalNAca1-4Galb1-3(Fuca1-2Galb1-4GlcNAcb1-GlcNAcb1-4(Mana1-3)Manb1-4GlcNAcb1-4(Fuca1- 6)GalNAca 6)GlcNAcGlcNAcb1-2Mana1-3Manb1-4GlcNAcb1-4(Fuca1-Fuca1-2Galb1-3(GlcNAca1-4Galb1-4GlcNAcb1- 6)GlcNAc 6)GalNAcGalNAca1-3(Fuca1-2)Galb1-3(Galb1-4GlcNAcb1-Fuca1-2Galb1-3GlcNAcb1-3Galb1-3(GlcNAcb1- 6GalNAc 6)GalNAcGalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3Galb1-GlcNAcb1-2Mana1-6Manb1-4GlcNAcb1-4(Fuca1- 3GalNAc 3)GlcNAcFuca1-4GlcNAcb1-3Galb1-3(Galb1-4GlcNAcb1-GlcNAcb1-2Mana1-6Manb1-4GlcNAcb1-4(Fuca1- 6)GalNAc 6)GlcNAcFuca1-2Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-3(Fuca1-2Galb1-4GlcNAcb1- 6)GalNAc 6)GalNAcFuca1-2Galb1-3GlcNAcb1-3(Galb1-4GlcNAcb1-GlcNAca1-4Galb1-3(Fuca1-2Galb1-4GlcNAcb1- 6)GalNAc 6)GalNAcFuca1-2Galb1-3/4GlcNAcb1-3Galb1-3(GlcNAcb1-Fuca1-4GlcNAcb1-6Galb1-3(Galb1-4GlcNAcb1- 6)GalNAc 6)GalNAcFuca1-3(Gal[3S]b1-4)GlcNAcb1-3(NeuAca2-GlcAb1-3Galb1-3(GlcNAcb1-3(Fuca1-4)GlcNAcb1- 6)GalNAc 6)GalNAcGlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-Galb1-3GalNAca1-4Galb1-3GalNAca1-4Galb1- 4GlcNAc 3GalNAcGalb1-4GlcNAcb1-6Galb1-3(Galb1-4GlcNAcb1-Galb1-3GlcNAcb1-3Galb1-3GlcNAcb1-3Galb1- 6)GalNAc 3GalNAcGalb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1- 4GlcNAcb 4GlcNAcbMana1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Manb1- 4GlcNAc 4GlcNAcGlcNAcb1-4(Mana1-3)(Mana1-6)Manb1-4GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1- 4GlcNAc 2Mana1-6)ManGalb1-3GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1- 3GalNAc 4GlcNAcbGalb1-3GlcNAcb1-3Galb1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1- 6)GalNAc 3GalNAcGlcNAcb1-4Mana1-3(Mana1-6)Manb1-4GlcNAcb1-Galb1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1- 4GlcNAc 6)GalNAcGalb1-4GlcNAcb1-3Galb1-3(Galb1-4GlcNAcb1-GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1- 6)GalNAc 4GlcNAcGalb1-4GlcNAcb1-2Mana1-6Manb1-4GlcNAcb1-Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGlcNAcb1-4(Mana1-3)(Mana1-6)Manb1-4GlcNAcb1-Galb1-3(Galb1-3GlcNAcb1-3Galb1-4GlcNAcb1- 4GlcNAcb 6)GalNAcMana1-3(GlcNAcb1-6Mana1-6)Manb1-4GlcNAcb1-NeuAca2-3Galb1-3(Galb1-4GlcNAc[6S]b1-6)GalNAc 4GlcNAcGalb1-3(Fuca1-2)Galb1-3(Fuca1-3GlcNAc[3S]b1-Galb1-3Galb1-3(NeuAca2-8NeuAca2-6)GalNAca 6)GalNAcGalNAcb1-4(NeuAca2-8NeuAca2-3)Galb1-4GlcbGalNAcb1-4(NeuAca2-8NeuAca2-3)Galb1-4GlcGalNAcb1-4(NeuAca2-8NeuAca2-3)Galb1-4GlcbGalNAcb1-4(NeuAca2-8NeuAca2-3)Galb1-4GlcGalNAcb1-4(NeuAca2-8NeuAca2-3)Galb1-4GlcFuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3(Kdna1- 6GalNAcGalb1-3(Fuca1-2)Galb1-3(NeuAca2-6)(Fuca1-Fuca1-2Galb1-3(Fuca1-2)Galb1-3(NeuAca2- 2)GalNAc 6)GalNAcGalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1- GalNAca1-3(Fuca1-2)Galb1-3(GlcNAcb1-3(GlcNAcb1-6)GalNAc 3GlcNAcb1-6)GalNAcNeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4GlcGala1-3Gala1-3Gala1-3Gala1-3Gala1-4Galb1-4GlcbGlcNAcb1-2(GlcNAcb1-4)Mana1-3Manb1-GlcNAca1-4Galb1-3(GlcNAca1-4Galb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc 6)GalNAcGalb1-4GlcNAcb1-3(GlcNAcb1-6)Galb1-4GlcNAcb1-GlcNAcb1-4Galb1-3(GlcNAca1-4Galb1-4GlcNAcb1- 3GalNAc 6)GalNAcGalNAca1-4Galb1-3(GalNAca1-4Galb1-4GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)Manb1- 6)GalNAca 4GlcNAcb1-4GlcNAcGalNAcb1-4GlcNAcb1-2Mana1-3Manb1-4GlcNAcb1-GlcNAcb1-3Galb1-3GlcNAcb1-3Galb1-3GlcNAcb1- 4GlcNAc 3GalNAcGalb1-4Galb1-3(NeuGca2-8NeuGca2-6)GalNAcGala1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcb1- 3Galb1-4GlcbNeuAca2-6Galb1-4GlcNAcb1-3(NeuAca2-6)GalNAcGalNAcb1-4(NeuAca2-3)Galb1-3(NeuAca2- 6)GalNAcNeuAca2-3Galb1-4GlcNAcb1-3(NeuAca2-6)GalNAcGalb1-4(NeuAca2-6)GlcNAcb1-3(NeuAca2-6)GalNAcGalNAca1-4(NeuAca2-3)Galb1-3(NeuAca2-Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3(NeuAca2- 6)GalNAc 6)GalNAcGalNAcb1-4GlcNAcb1-3(GalNAcb1-4(Fuca1-NeuAca2-3Galb1-3(Fuca1-2Galb1-4GlcNAcb1- 3)GlcNAcb1-6)GalNAc 6)GalNAcFuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3(NeuGca2-Kdna1-3Galb1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1- 6)GalNAc 6)GalNAcFuca1-2Galb1-3GalNAca1-4Galb1-3(NeuAca2-Fuca1-2Galb1-3GalNAca1-4(NeuAca2-3)Galb1- 6)GalNAc 3GalNAcNeuAca2-3Galb1-3(Galb1-3(Fuca1-4)GlcNAcb1-NeuAca2-3Galb1-3(Galb1-4(Fuca1-3)GlcNAcb1- 6)GalNAc 6)GalNAcaGalb1-3(NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-Galb1-3(NeuAca2-3Galb1-3(Fuca1-4)GlcNAcb1- 6)GalNAca 6)GalNAcNeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-NeuAca2-3Galb1-3(Fuca1-4)GlcNAcb1-3Galb1- 4GlcNAcb 3GalNAcFuca1-2Galb1-3(NeuAca2-3Galb1-4GlcNAcb1-NeuAca2-6Galb1-4GlcNAcb1-3Galb1-4(Fuca1- 6)GalNAc 3)GlcNAcGalb1-3(NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-3(NeuAca2- 6)GalNAc 6)GalNAcNeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-NeuAca2-3Galb1-3(Galb1-4(Fuca1-3)GlcNAcb1- 3GalNAc 6)GalNAcFuca1-2Galb1-3(Fuca1-2Galb1-4(Fuca1-Fuca1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1- 3)GlcNAcb1-6)GalNAc4(Fuca1-3)GlcNAcb Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3Galb1- 4(Fuca1-3)GlcNAcb4(Fuca1-3)GlcNAcb Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-GlcNAcb1-2Mana1-3(Man[6S]a1-6)Manb1- 4(Fuca1-3)GlcNAcb 4GlcNAcb1-4GlcNAcGalb1-4GlcNAc[6S]b1-3Galb1-4GlcNAcb1-3Galb1-Galb1-4GlcNAc[6S]b1-3Galb1-4GlcNAcb1-3Galb1- 3GalNAc 3GlcNAcMana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-Mana1-2Mana1-2Mana1-3(Mana1-3Mana1- 6)Manb1-4GlcNAc 6)Manb1-4GlcNAcMana1-2Mana1-3(Mana1-3(Mana1-6)Mana1-Mana1-2Mana1-3(Mana1-2Mana1-3Mana1- 6)Manb1-4GlcNAc 6)Manb1-4GlcNAcMana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-Mana1-3(Mana1-2Mana1-3(Mana1-6)Mana1- 4GlcNAcb1-4Glc 6)Manb1-4GlcNAcMana1-2Mana1-3(Mana1-2Mana1-2Mana1-Mana1-3(Mana1-3(Mana1-6Mana1-6)Mana1- 6)Manb1-4GlcNAc 6)Manb1-4GlcNAcMana1-3(Mana1-3(Mana1-2Mana1-6)Manb1-Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 6)Manb1-4GlcNAc 4GlcNAcb1-4GlcbMana1-6Mana1-3(Mana1-3(Mana1-6)Mana1-Glca1-3Mana1-3(Mana1-3(Mana1-6)Mana1- 6)Manb1-4GlcNAc 6)Manb1-4GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-6Manb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6Manb1- 4GlcNAc 4GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3Manb1-NeuAca2-3Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1- 4GlcNAc 6)ManNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3Manb1-NeuAca2-3Galb1-3(Gala1-3Galb1-4GlcNAcb1- 4GlcNAc 6)GalNAcGalb1-4GlcNAcb1-2(NeuAca2-3Galb1-4GlcNAcb1-NeuAca2-3Galb1-3GlcNAcb1-2Mana1-3Manb1- 6)Man 4GlcNAcNeuAca2-3Galb1-3(Gala1-3Galb1-4GlcNAcb1- 6)GalNAca1-1NeuAca2-3Galb1-3(Gala1-3Galb1-4GalNAcb1-Fuca1-3GalNAcb1-3Galb1-4Galb1-3(NeuGca2- 6)GalNAc 6)GalNAcFuca1-3GlcNAcb1-2Mana1-3(Fuca1-3GlcNAcb1-GalNAca1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcb1- 2Mana1-6)Man 3Galb1-4GlcbMana1-3Mana1-6Manb1-4GlcNAcb1-4(Fuca1-GalNAca1-3(Fuca1-2)Galb1-3(Fuca1-4)GlcNAcb1- 3)(Fuca1-6)GlcNAc3Galb1-4Glc Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 3)(Fuca1-6)GlcNAcb3)(Fuca1-6)GlcNAc GalNAca1-3(Fuca1-2)Galb1-3(Fuca1-4)GlcNAcb1-Gala1-4(Fuca1-2)Galb1-3(Fuca1-2)Galb1- 3Galb1-4Glcb 3(GlcNAcb1-6)GalNAcMana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-NeuAca2-8NeuAca2-8NeuAca2-3Galb1-4Glcb 3)(Fuca1-6)GlcNAcNeuAca2-8NeuAca2-8NeuAca2-3Gala1-4GlcbNeuAca2-8NeuAca2-8NeuAca2-3Galb1-4GlcbNeuAca2-8NeuAca2-8NeuAca2-3Galb1-4GlcbMana1-3(Mana1-3Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcMana1-3Mana1-3(Mana1-6)Mana1-4GlcNAcb1-Mana1-3(Mana1-6)Mana1-3Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc 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Mana1-3(Mana1-6)Mana1-3(Mana1-6)Manb1-GlcNAcb1-4(Mana1-3)(Mana1-3(Mana1-6)Mana1- 4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAc Mana1-3(Mana1-6)Mana1-3(Mana1-6)Manb1-Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAcbb Mana1-2(Mana1-3(Mana1-6)Mana1-6)Manb1-Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc GlcNAcb1-3Mana1-3(Mana1-3(Mana1-6)Mana1-GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1- 6)Manb1-4GlcNAc 6)Manb1-4GlcNAcMana1-2Mana1-3(Mana1-6Mana1-6)Manb1-Mana1-3(Mana1-2Mana1-3Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc Mana1-6Mana1-3Mana1-6Mana1-3Manb1-Mana1-3Glca1-6(Mana1-2Mana1-3)Glcb1- 4GlcNAcb1-4GlcNAc 4GlcNAcb1-4GlcNAcGlca1-3Mana1-2Mana1-2Mana1-3Manb1- Mana1-3(Mana1-2Mana1-6Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcb1-4GlcNAc Mana1-2Mana1-3(Mana1-6)Mana1-6Manb1-Mana1-3(Mana1-2Mana1-6)Mana1-6Manb1- 4GlcNAcb1-4GlcNAc 4GlcNAcb1-4GlcNAcMana1-2Mana1-3(Mana1-3Mana1-6)Manb1-GalNAcb1-4(NeuAca2-3)GalNAcb1-4Galb1-4Galb1- 4GlcNAcb1-4GlcNAcb 3GalNAcaGalb1-3GlcNAcb1-3(NeuAca2-3Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3(NeuAca2- 6)GalNAc 6)GalNAcNeuAca2-3Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-3(NeuAca2-3Galb1-4GlcNAcb1- 6)GalNAc 6)GalNAcGalb1-3(GalNAcb1-4(NeuAca2-3)Galb1-4GlcNAcb1-GalNAca1-3Galb1-3(NeuAca2-3Galb1-4GlcNAcb1- 6)GalNAc 6)GalNAcGalb1-3(NeuAca2-3Galb1-4GlcNAcb1-6)GalNAca1-GalNAcb1-4(NeuAca2-3)GalNAcb1-3Galb1-4Galb1- 3GalNAc 3GalNAcGalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-3(NeuGca2-GalNAcb1-4(NeuAca2-3)Galb1-3GalNAca1-4Galb1- 6)GalNAc 3GalNAcFuca1-2Galb1-4/3GlcNAcb1-3(Fuca1-2Galb1-Fuca1-2Galb1-3(GalNAca1-3(Fuca1-2)Galb1- 4/3GlcNAcb1-6)GalNAc4GlcNAcb1-6GalNAc Fuca1-2Galb1-3(Fuca1-4)GlcNAcb1-3Galb1-Fuca1-2Galb1-3/4GlcNAcb1-3(Fuca1-2Galb1- 3(GlcNAcb1-6)GalNAc3/4GlcNAcb1-6)GalNAc Galb1-4GlcNAcb1-3(Fuca1-2Galb1-4(Fuca1-Fuca1-3GlcNAcb1-2Mana1-6Manb1-4GlcNAcb1- 3)GlcNAcb1-6)GalNAc4(Fuca1-6)GlcNAcb Fuca1-3GlcNAcb1-2Mana1-3Manb1-4GlcNAcb1-Fuca1-2Galb1-3GlcNAcb1-3(Fuca1-2Galb1- 4(Fuca1-6)GlcNAcb4GlcNAcb1-6)GalNAc Neua1-6Galb1-4GlcNAcb1-2Mana1-3(Mana1-NeuAca2-3Galb1-3(NeuAca2-8NeuAca2-6)GalNAca 6)Manb1-4GlcNAcNeuAca2-8NeuAca2-3Galb1-3(NeuAca2-6)GalNAcNeuAca2-3Galb1-3(NeuAca2-8NeuAca2-6)GalNAcGalNAcb1-4(NeuGca2-3)GalNAcb1-3Galb1-4Galb1-GalNAcb1-4(NeuGca2-3)GalNAcb1-4Galb1-3Galb1- 3GalNAc 3GalNAcaGlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcb Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-Galb1-4GlcNAcb1-4Mana1-3Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAcb Mana1-3(GlcNAcb1-6Mana1-6)Manb1-4GlcNAcb1-Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc GlcNAcb1-2Mana1-3(Man[6PN]a1-6)Manb1-GlcNAc[6PN]b1-2Mana1-3(Man[6PN]a1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-Galb1-3(Fuca1-2Galb1-3GlcNAcb1-3Galb1- 4(Fuca1-6)GlcNAcb4GlcNAcb1-6)GalNAc Galb1-4GlcNAcb1-4Mana1-3Manb1-4GlcNAcb1-Fuca1-2Galb1-3GlcNAcb1-3Galb1-3(Galb1- 4(Fuca1-6)GlcNAc4GlcNAcb1-6)GalNAc Galb1-4GlcNAcb1-6Mana1-6Manb1-4GlcNAcb1-GlcNAcb1-4(Mana1-3)(Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc Galb1-3(Galb1-3GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-6)GalNAc Galb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6Manb1-GlcNAcb1-4Mana1-3(Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-3(Galb1-GlcNAcb1-4Mana1-3(Mana1-6)Manab1-4GlcNAcb1- 4GlcNAcb1-6)GalNAc4(Fuca1-6)GlcNAcb Galb1-4GlcNAcb1-2Mana1-6Manb1-4GlcNAcb1-GlcNAcb1-2(Mana1-3)(Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAcb GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-3)GlcNAc4(Fuca1-6)GlcNAc GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-GalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3Galb1- 4(Fuca1-6)GlcNAc3(Galb1-6)GalNAc Galb1-4GlcNAcb1-2Mana1-6Manb1-4GlcNAcb1-Mana1-3(GlcNAcb1-6Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc GlcNAcb1-2Mana1-2(Mana1-6)Manb1-4GlcNAcb1-Fuca1-2Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc3Galb1-4GlcNAcb Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-Fuca1-2Galb1-4GlcNAcb1-3(Fuca1-3Fuca1-4Kdna1- 4(Fuca1-6)GlcNAc 6)GalNAcGalb1-4GlcNAcb1-4Mana1-3(Mana1-6)Manb1-Galb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Mana1-3(Galb1-4GlcNAcb1-6Mana1-6)Manb1- 3Manb1-4GlcNAc4GlcNAcb1-4GlcNAcb GlcNAcb1-2Mana1-3(Mana1-3Mana1-6)Manb1-Galb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAcb Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-Galb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-4Mana1-3(Mana1-6)Manb1-Mana1-3(Galb1-4GlcNAcb1-4Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-GlcNAcb1-2Mana1-3(Mana1-3Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-Galb1-4GlcNAcb1-4Mana1-3(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAcb GlcNAcb1-2Mana1-3(Mana1-3/6Mana1-6)Manb1-GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1- 4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAc GalNAca1-3GalNAcb1-3(Galb1-3GalNAcb1-4)Gala1-4Galb1-4Glcb GlcNAcb1-2Mana1-3(Mana1-6Mana1-6)Manb1-Galb1-3GlcNAcb1-4Mana1-3(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc GlcNAcb1-2Mana1-3(Mana1-2Mana1-6)Manb1-GlcNAcb1-2Mana1-3(Mana1-6Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc Galb1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-Galb1-3GlcNAcb1-2Mana1-3(Mana1-6)Manb1- 3Galb1-3GalNAc 4GlcNAcb1-4GlcNAcGlcNAcb1-2Mana1-3(Mana1-3Mana1-6)Manb1-Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1- 4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAc Mana1-3(Galb1-4GlcNAcb1-4Mana1-6)Manb1-Galb1-3GalNAcb1-4(NeuAca2-8NeuAca2-3)Galb1- 4GlcNAcb1-4GlcNAcb 4GlcbNeuAca2-3Galb1-3GalNAcb1-4(NeuAca2-3)Galb1-NeuAca2-4Galb1-3(NeuAca2-6)GlcNAcb1-3Galb1- 4Glcb 4GlcNeuAca2-3Galb1-3(NeuAca2-6)GlcNAcb1-3Galb1-NeuAca2-8NeuAca2-3Galb1-3GalNAcb1-4Galb1- 4Glc 4GlcbFuca1-4Kdna1-3Galb1-3(Fuca1-2Galb1-4GlcNAcb1-Gala1-4(Fuca1-2)Galb1-4GlcNAcb1-3(Fuca1- 6)GalNAc 4Kdna1-6)GalNAcFuca1-4Kdna1-3Galb1-3(Fuca1-2Galb1-4GlcNAcb1-GalNAca1-3(Fuca1-2)Galb1-4GlcNAca1-3Galb1- 6)GlcNAcb 4GlcNAcb1-3GalNAcGalNAcb1-4GlcNAcb1-2Mana1-3Manb1-4GlcNAcb1-GalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-3Galb1- 4(Fuca1-6)GlcNAc4GlcNAcb1-3GalNAc GlcNAcb1-4(GlcNAcb1-2Mana1-3)Manb1-Galb1-3(NeuGca2-8NeuGca2-8NeuGca2-6)GalNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-3Galb1-3GalNAcb1-4(NeuGca2-3)Galb1-Galb1-3GalNAcb1-4(NeuAca2-8NeuGca2-3)Galb1- 4Glcb 4GlcbNeuGca2-3Galb1-3GalNAcb1-4(NeuAca2-3)Galb1-NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3(NeuAca2- 4Glcb 6)GalNAcGalNAcb1-4(Fuca1-3)GlcNAcb1-3(Fuca1-2Fuca1-GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1- 4Kdna1-6)GalNAc4GlcNAcb1-4GlcNAc GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAcb GlcNAcb1-4(Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 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GlcNAcb1-4Mana1-3(GlcNAcb1-6Mana1-6)Manb1-GlcNAcb1-4Mana1-3(GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-6)Manb1-GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-GlcNAcb1-2Mana1-3(GlcNAcb1-2(GlcNAcb1- 4GlcNAcb1-3GalNAc4)Mana1-6)Manb1-4GlcNAc GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-6)Manb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-3/4Galb1-3(Galb1-4GlcNAcb1-3Galb1-GlcNAca1-4(GlcNAca1-4(GlcNAca1-4GlcAa1- 4GlcNAcb1-6)GalNAc2)GlcAa1-2)GlcAa1-2Gal NeuGca2-3Galb1-3GalNAcb1-4(NeuGca2-3)Galb1-Galb1-3GalNAcb1-4(NeuGca2-8NeuGca2-3)Galb1- 4Glcb 4GlcbNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Mana1-GalNAcb1-4(Fuca1-3)GlcNAcb1-3(GalNAcb1- 6)Manb1-4Glcb4(Fuca1-3)GlcNAcb1-6)GalNAc NeuAca2-3Galb1-3(NeuAca2-3Galb1-4GlcNAcb1-6)GalNAc NeuAca2-3Galb1-4GlcNAcb1-3Galb1-3(NeuAca2-NeuAca2-3Galb1-3(NeuAca2-6Galb1-4GlcNAcb1- 6)GalNAca 6)GalNAcNeuAca2-3Galb1-3(NeuAca2-3Galb1-4GlcNAcb1-NeuAca2-3Galb1-3(NeuAca2-3Galb1-4GlcNAcb1- 6)GlcNAca 6)GalNAcaNeuAca2-3Galb1-3(NeuAca2-3Galb1-4GlcNAcb1-NeuAca2-3Galb1-3(NeuAca2-3Galb1-4GlcNAcb1- 6)GalNAca 6)GalNAcaNeuAca2-3Galb1-4GlcNAcb1-3Galb1-3(NeuAca2-NeuAca2-3Galb1-3(NeuAca2-3Galb1-4GlcNAcb1- 6)GalNAca 6)GalNAcaGalNAcb1-4Galb1-3Galb1-3(NeuAca2-8NeuAca2-GalNAca1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcb1- 6)GalNAca 3(Kdna1-6)GalNAcNeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-Fuca1-2Galb1-3(NeuAca2-3Galb1-4(Fuca1- 4(Fuca1-3)GalNAc3)GlcNAcb1-6)GalNAc NeuAca2-3Galb1-3(Fuca1-4)GlcNAcb1-3Galb1-NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1- 4(Fuca1-3)GlcNAc4(Fuca1-3)GlcNAc NeuAca2-3Galb1-3(Fuca1-2Galb1-4(Fuca1-GalNAcb1-3(Fuca1-2)Galb1-4GlcNAcb1-3(Fuca1- 3)GlcNAcb1-6)GalNAc4Kdna1-6)GalNAc NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1- 4(Fuca1-3)GlcNAcb4(Fuca1-3)GlcNAc Fuca1-3GalNAcb1-3Galb1-3GalNAcb1-4(NeuAca2-Man[6P]a1-2Mana1-3(Mana1-6(Man[6P]a1- 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6)Manb1-4GlcNAcMana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-Galb1-3(Fuca1-4)GlcNAcb1-3Galb1-3(Fuca1- 6)Manb1-4GlcNAc4)GlcNAcb1-3Galb1-4Glcb GlcNAcb1-3(NeuAca2-6)Galb1-4GlcNAcb1-NeuAca2-3Galb1-4GlcNAcb1-6(NeuAca2- 3(NeuAca2-6)GalNAc3GalNAcb1-3)GalNAca NeuAca2-3Galb1-4GlcNAcb1-6(NeuAca2-Galb1-3(Galb1-4(Fuca1-3)GlcNAcb1-6)GalNAcb1- 3GalNAcb1-3)GalNAca3Gala1-4Galb1-4Glcb Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcb4GlcNAcb1-4(Fuca1-6)GlcNAc Mana1-3(Mana1-3(Mana1-6)Mana1-6)Mana1-Gala1-3(Fuca1-2)Galb1-4GlcNAcb1-3Galb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcb4GlcNAcb1-3Galb1-4Glcb GlcNAcb1-2Mana1-3(Man[6PE]a1-6)Manb1-Fuca1-2Galb1-3GlcNAcb1-3(NeuAca2-3Galb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-6)GalNAc Galb1-4GlcNAcb1-3(NeuAca2-3Galb1-4(Fuca1-Fuca1-2Galb1-3(GalNAcb1-4(NeuAca2-3)Galb1- 3)GlcNAcb1-6)GalNAc4GlcNAcb1-6)GalNAc Fuca1-2Galb1-4GlcNAcb1-3(Fuca1-2Galb1-4(Fuca1-Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3(Fuca1- 3)GlcNAcb1-6)GalNAc2Galb1-4GlcNAcb1-6)GalNAc 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3Fuca1-4Kdna1-6)GalNAc3Manb1-4GlcNAcb1-4GlcNAc GlcNAca1-2Mana1-3(Mana1-3(Mana1-6)Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1- 6)Manb1-4GlcNAcb1-4GlcNAc2Mana1-6)Manb1-4GlcNAc GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Mana1-3Mana1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1- 6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Man Galb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Mana1-2Mana1- 2Mana1-6)Manb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAcb Galb1-4GlcNAcb1-2Mana1-3(Mana1-3Mana1-GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAcb1-4GlcNAc GlcNAca1-2Mana1-3(Mana1-3(Mana1-6)Mana1-GlcNAcb1-4(GlcNAcb1-3Mana1-3)(Mana1-3(Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Mana1-6)Manb1-4GlcNAc Galb1-4GlcNAcb1-2Glca1-3(Galb1-4GlcNAcb1-GlcNAcb1-4(Mana1-3)(Mana1-3(Mana1-6)Mana1- 2Glca1-6)Glcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc 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6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAc[6PN]b1-2Mana1-3(GlcNAcb1-2Man[6PN]a1-GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcbGalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1-GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc Fuca1-2Galb1-4GlcNAca1-3Galb1-3/6(GlcNAcb1-GlcNAcb1-3/4/2Galb1-6/3(Fuca1-2Galb1- 4/2Galb1-4GlcNAcb1-6/3)GalNAc4GlcNAcb1-3Galb1-4GlcNAcb1-3/6)GalNAcGalb1-4Galb1-3(NeuGca2-8NeuGca2-8NeuGca2- 6)GalNAcFuca1-4(Fuca1-5)Kdna1-3Galb1-3(Fuca1-4(Fuca1-Fuca1-4(Fuca1-5)Kdna1-3Galb1-3(Fuca1-4(Fuca1- 5)Kdna1-6)GlcNAcb5)Kdna1-6)GalNAc Glcb1-4Glcb1-4Glcb1-4Glcb1-4Glcb1-4Glcb1-Fuca1-3GalNAcb1-4Galb1-3Galb1-3(NeuAca2- 4Glcb1-4Glcb1-4Glcb8NeuAca2-6)GalNAca NeuAca2-3Galb1-3(NeuAca2-3Galb1-4(Fuca1-NeuAca2-3Galb1-3(NeuAca2-3Galb1-4(Fuca1- 3)GlcNAcb1-6)GalNAc3)GlcNAcb1-6)GalNAca NeuAca2-3Galb1-3(NeuAca2-3Galb1-4(Fuca1-Fuca1-3Fuca1-4Kdna1-3Galb1-3(GalNAcb1- 3)GlcNAcb1-6)GalNAca4(Fuca1-3)GlcNAcb1-6)GalNAc GalNAcb1-3(Fuca1-2)Galb1-4GlcNAcb1-3(Fuca1-Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1- 3Fuca1-4Kdna1-6)GalNAc6)Manb1-4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-Galb1-3GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1- 6)Manb1-4GlcNAcb1-4GlcNAcb3(Galb1-4GlcNAcb1-6)GalNAc Galb1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1- 3Galb1-4GlcNAcb1-6)GalNAc3(Galb1-4GlcNAcb1-6)GalNAc Galb1-4GlcNAcb1-4Mana1-3(GlcNAcb1-2Mana1-GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-2Mana1- 6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAcb GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-4Mana1-3(GlcNAcb1-2Mana1- 6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAcb GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-2Manb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1- 6)Mana1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Mana1-4GlcNAc 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6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1- 4GlcNAcb1-3Galb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc NeuAca2-3Galb1-4GlcNAc[6S]b1-3Galb1-NeuAca2-3Galb1-4GlcNAcb1-2(NeuAca2-3Galb1- 4GlcNAcb1-3Galb1-3GalNAc4GlcNAcb1-6)Man NeuGca2-3Galb1-4GlcNAc[6S]b1-3Galb1-GlcNAcb1-4(GlcNAcb1-2(Fucb1-4GlcNAcb1- 4GlcNAcb1-3Galb1-3GalNAc4)Mana1-3)Manb1-4GlcNAcb1-4GlcNAcb GlcNAcb1-4(GalNAcb1-4GlcNAcb1-2Mana1-GlcNAc[6PE]b1-2Mana1-3(Man[6PE]a1-6)Manb1-3)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAc[6S]b1-3Gal[6S]b1-4GlcNAc[6S]b1-Fuca1-3GalNAcb1-3Galb1-4Galb1-3(NeuGca2- 3Gal[6S]b1-4GlcNAc[6S]b1-3Gal8NeuGca2-6)GalNAc Man[6P]a1-2Mana1-3(Mana1-2Mana1-Man[6P]a1-2Mana1-3(Mana1-3(Man[6P]a1-6(Man[6P]a1-3)Mana1-6)Manb1-4GlcNAc 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3(Galb1-4GlcNAcb1-2Mana1-6)ManGalb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 2(Galb1-4GlcNAcb1-6)Mana1-6)ManNeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-Fuca1-2Galb1-3GlcNAcb1-3(Fuca1-2Galb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAcb3GlcNAcb1-6)Galb1-3(GlcNAcb1-6)GalNAcGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-GalNAca1-3(Fuca1-2)Galb1-3(Galb1-3GlcNAca1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 3(Fuca1-2)Galb1-4GlcNAcb1-6)GalNAcGlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-4GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcFuca1-2Galb1-3GlcNAcb1-3(Fuca1-2Galb1-GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-4GlcNAcb1-6)Galb1-3(GlcNAcb1-6)GalNAc6)Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcbGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-Galb1-3(NeuGca2-8NeuGca2-8NeuGca2-8NeuGca2-6)Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAc 6)GalNAcNeua1-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-Neua1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1- 3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcGalNAcb1-4Galb1-3Galb1-3(NeuAca2-8NeuAca2-Fuca1-2(Fuca1-3)Fuca1-4Kdna1-3Galb1- 8NeuAca2-6)GalNAca3(GalNAcb1-4(Fuca1-3)GlcNAcb1-6)GalNAcGalb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-3Mana1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalNAcb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)Man 3)(Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-2Glca1-3(Galb1-4GlcNAcb1-2Glca1-GlcNAcb1-4(Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GlcNAcb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalb1-3GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-GlcNAcb1-2Mana1-3(Gala1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-4Mana1-Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcFuca1-2Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-Fuca1-2Galb1-3GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 6)Galb1-3(Galb1-4GlcNAcb1-6)GalNAcFuca1-2Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-3Mana1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Mana1-Galb1-4GlcNAc[6S]b1-3Galb1-4GlcNAc[6S]b1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 3Galb1-4GlcNAcb1-3Galb1-3GalNAcGlca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-Fuca1-4(Fuca1-5)Kdna1-3Galb1-3(GalNAca1- 3(Mana1-2Mana1-3Mana1-6)Man3(Fuca1-2)Galb1-4GlcNAcb1-6)GalNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-Galb1-3GlcNAcb1-2Mana1-3(Galb1-3GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-3GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcMana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 2Mana1-6)Manb1-4GlcNAcb1-3GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-6Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-3GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Mana1-4GlcNAcb1-4GlcNAcbb 4Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-2Mana1-3(GlcNAcb1-4(Mana1-3)(Mana1-Glcb1-4GlcNAcb1-2Mana1-3(Glcb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-3Mana1-3)(Mana1-3(Mana1-GlcNAcb1-2Mana1-3(Gala1-3Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 3Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(Mana1-3)(GlcNAcb1-2Mana1-3(Mana1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalNAca1-3(Fuca1-2)Galb1-3(GalNAca1-3(Fuca1-GalNAcb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-2)Galb1-4GlcNAcb1-3GlcNAcb1-6)GalNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-2Mana1-3(GalNAcb1-4GlcNAcb1-2Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-2Mana1-3(GlcNAcb1-2(GlcNAcb1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-GlcNAcb1-2Mana1-3(GlcNAcb1-2(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-2Mana1-3(GlcNAcb1-2(GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb2Mana1-6)Mana1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb6)GlcNAcb1-4Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-3)(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-GlcNAcb1-2(GlcNAcb1-6)Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-GalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-3Galb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb4GlcNAcb1-3Galb1-4GlcNAcb1-3GalNAc GalNAc[4S]b1-4GlcNAcb1-2Mana1-Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(GalNAc[4S]b1-4GlcNAcb1-2Mana1-6)Manb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAc 4GlcNAcMana1-2Mana1-2Mana1-3(Mana1-3(Mana1-Mana1-3Mana1-2Mana1-2(Mana1-6)Mana1-2(Mana1-6)Mana1-6)Mana1-6)Manb1-4GlcNAc3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcMana1-3Mana1-2Mana1-2Mana1-3(Mana1-Glcb1-3Mana1-2Mana1-2Mana1-3(Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAc 2Mana1-6)Mana1-6)Manb1-4GlcNAcGlca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-Mana1-2Mana1-3Mana1-3(Mana1-2Mana1- 2Mana1-3Mana1-6)Manb1-4GlcNAc3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcMana1-2Mana1-2Mana1-3(Mana1-2Mana1- Mana1-2Mana1-2Mana1-3(Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-3GlcNAc2Mana1-6Mana1-6)Mana1-6)Manb1-4GlcNAcGlca1-3Mana1-2Mana1-2Mana1-3(Mana1-3(Mana1-Mana1-2Mana1-2(Mana1-6)Mana1-3(Mana1- 2Mana1-6)Mana1-6)Manb1-4GlcNAc3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcMana1-2Mana1-2(Mana1-2Mana1-6)Mana1- 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GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-GlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(GlcNAcb1-GlcNAcb1-2Mana1-3(GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-4)Mana1-3)(Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(GalGalb1-4GlcNAcb1-2Mana1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1- GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcbGlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1- 3(Mana1-6)Mana1-6)Manb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcbNeuAca2-3Galb1-3GlcNAcb1-3Galb1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-3Galb1-3(NeuAca2- 3Galb1-4GlcNAcb1-6)GalNAc3Galb1-4GlcNAcb1-6)GalNAc Fuca1-2Galb1-3(Fuca1-2Galb1-4(Fuca1-GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(Mana1-3)GlcNAcb1-3(Fuca1-2)Galb1-4GlcNAcb1-3Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 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6)GalNAcNeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-3(Mana1-GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(GlcNAcb1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalNAc[4S]b1-4GlcNAcb1-2Mana1-3(GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Mana1-2(Mana1-Galb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(Mana1-2Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAcGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)(Fuca1-6)GlcNAcbMana1-2Mana1-2Mana1-3(Man[6P]a1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcMana1-2Man[6P]a1-2Mana1-3(Mana1-2Mana1-GalNAc[3S]b1-4GlcNAcb1-2Mana1-3(Galb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalNAc[4S]b1-4GlcNAcb1-2Mana1-3(Galb1-GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4Glcb3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcbMana1-2Mana1-3(Mana1-3(Mana1-2Mana1-Gala1-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-4GlcNAcb3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcMana1-2Mana1-2Mana1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcGlcNAcb1-4(GalNAcb1-4GlcNAcb1-2(GalNAcb1-Fuca1-3GalNAcb1-4Galb1-3Galb1-3(NeuAca2-4GlcNAcb1-4)Mana1-3)Manb1-4GlcNAcb1-4GlcNAc 8NeuAca2-8NeuAca2-6)GalNAcaNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbNeuAca2-3Galb1-3(Galb1-3GlcNAcb1-3(Galb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-4GlcNAcb1-6)Galb1-4GlcNAcb1-6)GalNAc3)(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(Mana1-3)(Galb1-4(Fuca1-3)GlcNAcb1-Fuca1-2Galb1-3GlcNAcb1-3(Fuca1-2Galb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc3GlcNAcb1-6)Galb1-3GlcNAcb1-3Galb1-3GalNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GlcNAcb1-Fuca1-2Galb1-3GlcNAcb1-3(Fuca1-2Galb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb3GlcNAcb1-6)Galb1-3(Galb1-4GlcNAcb1-6)GalNAcGalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3(Fuca1-Fuca1-2Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Galb1-3GlcNAcb1-6)Galb1-3(Galb1-6)GalNAc2Mana1-6Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcFuca1-2Galb1-3/4GlcNAcb1-3/6(Fuca1-2Galb1-Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4GlcNAcb1-3/4GlcNAcb1-6/3)Galb1-3(Galb1-4GlcNAcb1- 2Mana1-6Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 6)GalNAcGalb1-4Galb1-3(NeuGca2-8NeuGca2-8NeuGca2-NeuAca2-3Gal[6S]b1-4GlcNAcb1-3Galb1- 8NeuGca2-6)GalNAc3(NeuAca2-3Galb1-4GlcNAcb1-6)GalNAcNeua1-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb6Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-4Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 3 Mana1-6 Manb1-4GlcNAcb1-4Fuca1-6 GlcNAc 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6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalNAcb1-4GlcNAcb1-2Mana1-3(GalNAc[4S]b1-GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGalb1-3Galb1-4GlcNAcb1-3(Galb1-3Galb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-4GlcNAcb1-6)Galb1-4GlcNAcb1-3Galb1-3GalNAc2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAc3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Mana1-Gala1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAc3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-3Galb1-2(Gatb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-2cGalb1-4GlcNAcb1-4)Mana1-3(Mana1-GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-6Galb1-3GlcNAcb1-3(NeuAca2-6)Galb1-6Galb1-4GlcNAcb1-2Mana1-6)Man 4GlcNAcb1-3(NeuAca2-6)GalNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1- GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4(Fuca1-6)GlcNAcGlcNAcb1-2Mana1-3(GlcNAcb1-2(Galb1-3GlcNAcb1-GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1- GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4(Fuca1-6)GlcNAcb 6)GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 4(Fuca1-6)GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)GlcNAcbGalb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1- GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcGalb1-4GlcNAcb1-2Mana1-3(GalNAcb1-4GlcNAcb1-GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalNAcb1-4GlcNAcb1-2Mana1-3(GalNAcb1-GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-4GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)ManGlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcGlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1- 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4GlcNAcGlcb1-2Glcb1-2Glcb1-2Mana1-2Mana1-2Mana1-Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAc3(Mana1-2Mana1-6)Mana1-6)Manb1-3GlcNAcGlca1-3Mana1-2Mana1-2Mana1-3(Mana1-3Mana1-NeuAca2-3Galb1-3(NeuAca2-3Galb1-4(Fuca1-3(Mana1-3Mana1-6)Mana1-6)Manb1-4GlcNAc3)GlcNAcb1-3Galb1-4GlcNAcb1-6)GalNAcNeuAca2-3Galb1-3(NeuAca2-3Galb1-3(Fuca1-NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4)GlcNAcb1-3Galb1-4GlcNAcb1-6)GalNAc4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcbNeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcbNeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-4GlcNAcGlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcGlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-4)Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcGalb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb4)Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcbGlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 4GlcNAcbGalb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcGlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4)Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcGalb1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-6)GalNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-Gal[3ME]b1-6Gal[3ME]b1-3(Gal[3ME]b1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-3GalNAc6)GlcNAcb1-4GlcNAcb1-2Mana1-3(Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcGal[3ME]b1-6Gal[3ME]b1-3(Gal[3ME]b1-NeuAca2-6Galb1-4GlcNAcb1-2(NeuAca2-6Galb1-6)GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1- 4GlcNAcb1-4)Mana1-3Manb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc NeuAca2-6Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-NeuAca2-6Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-4GlcNAcb1-4)Mana1-3Manb1-4GlcNAc 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6)GlcNAcGlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc 4(Fuca1-6)GlcNAcbGalNAcb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcGalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-GalNAcb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GalNAca1-3Galb1-4GlcNAcb1-6)Galb1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-3GalNAc 4(Fuca1-6)GlcNAcMana1-3(GalNAcb1-4GlcNAcb1-2(GalNAcb1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAcb 4(Fuca1-6)GlcNAcbNeuAca2-8NeuAca2-3Galb1-3GalNAcb1-4(NeuAca2-NeuAca2-3Galb1-3GalNAcb1-4(NeuAca2-8NeuAca2- 8NeuAca2-3)Galb1-4Glcb8NeuAca2-3)Galb1-4Glcb GalNAcb1-4(NeuGca2-3)GalNAcb1-3Galb1-4Galb1-NeuAca2-8NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1- 3(NeuGca2-8NeuGca2-6)GalNAc3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAc GalNAc[4S]b1-4GlcNAcb1-2Mana1-GalNAc[3S]b1-4GlcNAcb1-2Mana1- 3(GalNAc[4S]b1-4GlcNAcb1-2Mana1-6)Manb1-3(GalNAc[3S]b1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-GlcNAcb1-4(Mana1-2Mana1-2Mana1-3)(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1- 4GlcNAcb 4GlcNAcMana1-2Mana1-2Mana1-3(Mana1-2Mana1- Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Mana1-4GlcNAcb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcbbMana1-2Mana1-2Mana1-3(Mana1-2Mana1-Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcGlca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcMana1-2Mana1-2Mana1-3(Mana1-2Mana1-Glca1-3Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 4GlcNAcMana1-3(Mana1-2Mana1-2Mana1-2Mana1-2Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlca1-3Mana1-2Mana1-2(Mana1-3Mana1-2Mana1-6)Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAcMana1-3Mana1-2Mana1-2(Mana1-3Mana1-2Mana1-Mana1-3Mana1-2Mana1-2Mana1-3(Mana1-6)Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcMana1-2Mana1-2(Mana1-6)Mana1-3(Mana1-Glca1-3Glca1-3Mana1-2Mana1-2(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-6)Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcbGalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3(NeuAca2-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1- 6)Galb1-4GlcNAcb1-3(NeuAca2-6)GalNAc3)(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcGlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1- Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-4)Mana1-3)(GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc 4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3)(GlcNAcb1-2Mana1-6)Manb1- 4)Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb 4GlcNAcb1-4GlcNAcGalNAcb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-4)Mana1-3(GlcNAcb1-2Mana1-6)Manb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc 4GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1-3)(GlcNAcb1-2(Mana1-6)Mana1-6)Manb1- 4GlcNAc 4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-4GlcNb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcMana1-3(Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Mana1-6Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Mana1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-2Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-NeuAca2-6GlcNAcb1-2Mana1-3(NeuAca2-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)GlcNAcbGalNAc[3S]b1-4GlcNAcb1-2Mana1-3(Galb1-GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcbGala1-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-GlcNAcb1-4(GalNAcb1-4GlcNAcb1-2(GalNAcb1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-4)Mana1-3)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcGalNAcb1-4Galb1-3Galb1-3(NeuAca2-8NeuAca2-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1- 8NeuAca2-8NeuAca2-6)GalNAca2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbNeuAca2-3Galb1-3GlcNAcb1-2Mana1-3(GlcNAcb1-GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-2Mana1-6)GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(NeuAca2-3/6Galb1-4GlcNAcb1-GlcNAcb1-4(NeuAca2-3/6Galb1-4(Fuca1-2Mana1-3)(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3)(Mana1-6)Manb1- 6)GlcNAc 4GlcNAcb1-4GlcNAcFuca1-2Galb1-3(Fuca1-4)GlcNAcb1-3(Fuca1-Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-2Galb1-3GlcNAcb1-6)Galb1-3(Galb1-4GlcNAcb1-3(Fuca1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GalNAc 4GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcbMana1-2Mana1-2Mana1-2Mana1-2Mana1-3(Galb1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcbGlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-3)(GlcNAcb1-2(GlcNAcb1-4)Mana1-6)Manb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAcb GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-3)(GlcNAcb1-2(GlcNAcb1-4)Mana1-6)Manb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(GlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-6)Manb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-3)(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-2(GalNAcb1-4GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GalNAcb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-GalNAcb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(GlcNAca1-2(GlcNAcb1-4)Mana1-GlcNAcb1-4(GlcNAcb1-4Mana1-3)(GlcNAcb1-3)(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-2Mana1-NeuAca2-3Galb1-4GlcNAc[6S]b1-3Galb1-6GlcNAcb1-4)Mana1-3)Manb1-4GlcNAcb1-4GlcNAc[6S]b1-3Galb1-4GlcNAcb1-3Galb1-3GalNAc 4GlcNAcb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-2Mana1-3(NeuGca2-6Galb1-4GlcNAcb1-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(Mana1-NeuAca2-3Galb1-3GlcNAcb1-2Mana1-3(Galb1-2Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcGalb1-3GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Galb1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4GlcNAcFuca1-2Galb1-4GlcNAcb1-2Mana1-3(Fuca1-2Galb1-Galb1-4GlcNAcb1-2Mana1-3(Fuca1-2Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcbGalb1-4GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-Gala1-3(Fuca1-2)Galb1-4GlcNAcb1-2Mana1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcFuca1-2Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(Fuca1-2Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcFuca1-2Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcNeuGca2-3Galb1-4GlcNAc[6S]b1-3Galb1-NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAc[6S]b1-3Galb1-4GlcNAcb1-3Galb1-3GalNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(NeuGca2-3/6Galb1-4GlcNAcb1-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-2Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcNeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Gala1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6GlcNAcbGalb1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcbGala1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcbGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Mana1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Galb1-4(Fuca1-3)GlcNAcb1-2(GlcNAcb1-4)Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4GlcNAcGalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-4GlcNAcb1-3(NeuAca2- 6)GalNAcNeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcbGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-4Galb1-4GlcNAcb1-2Mana1-3(Galb1-4Galb1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)ManGala1-3Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Gala1-3Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(Gala1-3Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGlcNAcb1-4(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbNeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-GlcNAcb1-4(NeuAca2-3/6Galb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc2Mana1-3)(GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(NeuAca2-GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcGlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GalNAcb1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4(Fuca1-6)GlcNAc 6)GlcNAcGalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3(Fuca1-GalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-3(Fuca1-2Galb1-3GlcNAcb1-6)Galb1-3(Galb1-4GlcNAcb1-2Galb1-3GlcNAcb1-6)Galb1-3GlcNAcb1-3Galb1- 6)GalNAc 3GalNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GalNAcb1-GlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1-4(Fuca1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4GlcNAc 6)GlcNAcGlcNAcb1-4(GlcNAcb1-2Mana1-3)(Galb1-4(Fuca1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcbGalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-2Mana1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4Glcb 6)GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4Glcb3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcbGalNAc[4S]b1-4GlcNAcb1-2Mana1-3(Gal[3S]b1-NeuAca2-3Galb1-3(NeuAca2-3Galb1-3(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-6)GalNAc 6)GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-GlcNAcb1-4(Galb1-4GlcNAcb1-4Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcbGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-Fuca1-6GlcNAcb1-4GlcNAcb1-4(Galb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-2Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1- 6)GlcNAc 4GlcNAcGalb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-4Mana1-3)(Galb1-Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-4Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcGlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcGlcNAcb1-2(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-GlcNAcb1-2/4Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcbGalb1-4GlcNAcb1-6(Galb1-4GlcNAcb1-2(Galb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-4(Fuca1-3)GlcNAcb1-3)Manb1-3)Manb1-2Mana1-6)GlcNAcb1-4Manb1-4GlcNAcb1-4(Fuca1- 4GlcNAcb1-4GlcNAcb 6)GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcbGala1-3Galb1-4GlcNAcb1-2Mana1-3(GalNAcb1-Neua1-6Galb1-4GlcNAcb1-2Mana1-3(Neua1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAcb 4GlcNAcNeua1-3Galb1-4GlcNAcb1-2Mana1-3(Neua1-NeuAca2-6Galb1-4GlcNAc[6S]b1-2Mana1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4GlcNAc 6)GlcNAcGlca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-Mana1-2Mana1-2(Mana1-6Mana1-6)Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-3(Mana1-3(Mana1-2Mana1-2Mana1-6)Mana1- 4GlcNAc 6)Manb1-4GlcNAcMana1-2Mana1-2(Mana1-6Mana1-6Mana1- Mana1-3Mana1-2Mana1-2(Mana1-6)Mana1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-3Mana1-2Mana1-6)Mana1- 6)Manb1-4GlcNAc 6)Manb1-4GlcNAcGlca1-2Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-Mana1-2Mana1-2(Mana1-2Mana1-6)Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1- 4GlcNAc 6)Manb1-4GlcNAcMana1-2Mana1-2(Mana1-2Mana1-6Mana1-Mana1-2Mana1-2(Mana1-2(Mana1-6)Mana1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1- 6)Manb1-4GlcNAc 6)Manb1-4GlcNAcMana1-3Mana1-2Mana1-2Mana1-3(Mana1-Glca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2(Mana1-2Mana1-6)Mana1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1- 6)Manb1-4GlcNAc 4GlcNAcMana1-3Mana1-2Mana1-2(Mana1-3Mana1-2Mana1-Mana1-3Mana1-2Mana1-2(Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1- 4GlcNAc 6)Manb1-4GlcNAcGlca1-2Glca1-3Glca1-3Mana1-2Mana1-2(Mana1-Glca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-3(Mana1-2Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAc 4GlcNAcGlcb1-2Glcb1-2Glcb1-2Mana1-2Mana1-2Mana1-Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1- 4GlcNAc 3GlcNAcNeuAca2-8NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAcNeuAca2-8NeuAca2-3/6Galb1-4GlcNAcb1-2Mana1-GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcbGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGalb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-3GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1-2(Galb1-3GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGlcNAcb1-4(Gala1-3Galb1-4GlcNAcb1-2Mana1-Galb1-3GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcGalb1-4GlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcGalb1-3GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAc 4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-3)Mana1-GlcNAcb1-4(Galb1-4GlcNAcb1-2(GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAcb 4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc 4GlcNAcNeuAca2-3Galb1-4GlcNAc[6S]b1-3Galb1-Gal[3S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAc[6S]b1-3Galb1-4GlcNAc[6S]b1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 3GalNAcGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(GalNAcb1-3(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc GalNAcb1-4GlcNAcb1-2Mana1-3(GalNAcb1-GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1- 4(Fuca1-6)GlcNAcb4GlcNAcb1-4(Fuca1-6)GlcNAcb GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-4(GalNAcb1-4(Fuca1-3)GlcNAcb1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1- 2Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-6)Manb1-4GlcNAcb1-4GlcNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-8NeuAca2-3/6Galb1-4GlcNAcb1-2Mana1-NeuAca2-8NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-3(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-8NeuGca2-3/6Galb1-4(Fuca1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3)GlcNAcb1-2Mana1-3(Mana1-6)Manb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAc 4GlcNAcb1-4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Manb1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-2Glca1-3(NeuAca2-6Galb1-4GlcNAcb1-2Manb1-6)Mana1-4GlcNAc3Galb1-4GlcNAcb1-2Glca1-6)Manb1-4GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-6Galb1-4GlcNAcb1-2Manb1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAc3Galb1-4GlcNAcb1-2Manb1-6)Mana1-4GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Glca1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-2Manb1-3(NeuAca2-6Galb1-4GlcNAcb1-2Glca1-6)Manb1-4GlcNAc3Galb1-4GlcNAcb1-2Manb1-6Mana1-4GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-3Galb1-3GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-4Mana1-6)Manb1-4GlcNAc3Galb1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcbGal[3ME]b1-6Gal[3ME]b1-3(Gal[3ME]b1-Gal[3ME]b1-6Gal[3ME]b1-3(Gal[3ME]b1-6Gal[3ME]b1-6)GalNAcb1-4GlcNAcb1-2Mana1-6Gal[3ME]b1-6)GlcNAcb1-4GlcNAcb1-2Mana1-3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 3(Mana1-6)Manb1-4GlcNAcb1-4GlcNAcNeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-NeuGca2-3Galb1-4GlcNAc[6S]b1-3Galb1-3(Mana1-3Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAc[6S]b1-3Galb1-4GlcNAc[6S]b1-3Galb1- 6)GlcNAc 3GalNAcGalNAc[4S]b1-4GlcNAcb1-2Mana1- GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(GalNAc[4S]b1-4GlcNAcb1-2Mana1-6)Manb1-3(GalNAc[4S]b1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAcb GalNAc[3S]b1-4GlcNAcb1-2Mana1-GlcNAcb1-3(NeuAca2-6)Galb1-4GlcNAcb1-3(GalNAc[3S]b1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-6)Galb1-4GlcNAcb1-3(NeuAca2- 4GlcNAcb1-4(Fuca1-6)GlcNAc6)GalNAc Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GlcNAcb1-4(Galb1-4GlcNAcb1-2(GlcNAcb1-Galb1-4(Fuca1-3)GlcNAcb1-2(GlcNAcb1-4)Mana1-4)Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3)(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-3)(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4)Mana1-3)(GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GalNAcb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1- 4)Mana1-3(GlcNAcb1-2Mana1-6)Manb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc GlcNAc[6S]b1-3Gal[6S]b1-4GlcNAc[6S]b1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Mana1-3Gal[6S]b1-4GlcNAc[6S]b1-3Gal[6S]b1-2Mana1-3Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4GlcNAc[6S]b1-3Gal 6)GlcNAcNeuAca2-3Galb1-4GlcNAcb1-3Mana1-3(Mana1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Mana1-Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAcb 4(Fuca1-6)GlcNAcbMana1-2Man[6P]a1-2Mana1-3(Mana1-2Mana1-Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-3(Mana1-2Man[6P]a1-6)Mana1-6)Manb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAcb 4GlcNAcMana1-2Mana1-2Mana1-3(Mana1-2Mana1-Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-2Mana1-6)Mana1-6)Manb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc 4GlcNAcGlca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcbMana1-2Mana1-2Mana1-2Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcbMana1-2Mana1-3(Mana1-2Mana1-2Mana1-6)Mana1-3(Mana1-2Mana1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcbGlca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-Mana1-2Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-3Mana1-6)Manb1-4GlcNAcb1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcMana1-3Mana1-2Mana1-2Mana1-3(Mana1-Glca1-3Glca1-3Mana1-2Mana1-2(Mana1-3Mana1-3(Mana1-3Mana1-2Mana1-6)Mana1-6)Manb1-2Mana1-6)Mana1-3(Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAcb 4GlcNAcMana1-3Mana1-2Mana1-2Mana1-3(Mana1-Glca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-3Mana1-2Mana1-6)Mana1-6)Manb1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc 4GlcNAcGlca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-Mana1-2Mana1-2(Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3(Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1- 4GlcNAcb 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4GlcNAcb1-4GlcNAcGlcNAc[3S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-GlcNAc[4S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcbGalNAc[4S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGalNAc[4S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-Gala1-3(Fuca1-2)Galb1-4GlcNAcb1-3(Gala1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Fuca1-2)Galb1-4GlcNAcb1-6)Galb1-4GlcNAcb1- 4GlcNAcb 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6)GlcNAcGalb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-Glcb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Glcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcGalb1-3GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-NeuAca2-3Galb1-4GlcNAca1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAca1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Galb1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-3)GlcNAcb Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Galb1-Galb1-4(Fuca1-3)GlcNAcb1-4Mana1-3(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc Galb1-4(Fuca1-3)GlcNAcb1-4Mana1-3(Galb1-Fuca1-2Galb1-4GlcNAcb1-2Mana1-3(Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4(Fuca1-6)GlcNAcb 6)GlcNAcbFuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcbFuca1-2Galb1-3GlcNAcb1-2Mana1-3(Fuca1-2Galb1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 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NeuGca2-8NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-GlcNAcb1-4(NeuGca2-8NeuGca2-3/6Galb1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-2Mana1-3)(Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4GlcNAc6)GlcNAc#pyridylamine NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-NeuAca2-6Gab1-4GlcNAcb1-2Mana1-3(Gala1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(NeuGca2-6Galb1-NeuAca2-6Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1- 6)GlcNAc#pyridylamine 4GlcNAcGala1-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-3/6Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGala1-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-3/6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3)GlcNAcb1-2Mana1-3)(Mana1-3Mana1-6)Manb1- 4GlcNAc 4GlcNAcb1-4GlcNAcGlcNAcb1-4(NeuGca2-3/6Galb1-4GlcNAcb1-GlcNAcb1-4(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-2Mana1-3)(Mana1-3Mana1-6)Manb1-4GlcNAcb1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc 4GlcNAcbGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(NeuGca2-NeuAca2-3/6Galb1-4GlcNAcb1-2(GlcNAcb1-3/6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4)Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAc 4GlcNAcb1-4GlcNAcGlcNAcb1-4(NeuAca2-3/6Galb1-4GlcNAcb1-NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-3(Galb1-2Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4GlcNAcb1-4GlcNAc 6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Gala1-Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-4)Mana1-3(Mana1-3Mana1-6)Manb1- 4(Fuca1-6)GlcNAcb4GlcNAcb1-4GlcNAc GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcb Galb1-4(Fuca1-3)GlcNAcb1-2(GlcNAcb1-4)Mana1-Gala1-3(Fuca1-2)Galb1-4GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Gala1-3(Fuca1-GalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-2Mana1-2)Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Mana1-2Mana1-3Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc GalNAca1-3Galb1-3GlcNAcb1-3(NeuAca2-6Galb1-GlcNAcb1-4(NeuGca2-3/6Galb1-4GlcNAcb1-4GlcNAcb1-6)Galb1-4GlcNAcb1-3(NeuAca2-2Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1- 6)GalNAc 4GlcNAcb1-4GlcNAcGala1-3Galb1-4GlcNAcb1-2Mana1-3(NeuGca2-GlcNAcb1-4(Gala1-3Galb1-4GlcNAcb1-2Mana1-3/6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4(Fuca1-6)GlcNAcGala1-3Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Galb1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcb 6)GlcNAcGala1-3Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4)Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 6)GlcNAc 4GlcNAcb1-4GlcNAcGala1-3Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAc 4(Fuca1-6)GlcNAcGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4(Fuca1-6)Glc 6)GlcNAcbGalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(GalNAcb1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcbGlcNAcb1-2(Galb1-3(NeuAca2-6)GlcNAcb1-GlcNAcb1-4(NeuAca2-3/6Galb1-4(Fuca1- 4)Mana1-3(GlcNAcb1-2Mana1-6)Manb1-3)GlcNAcb1-2Mana1-3)(GlcNAcb1-2Mana1- 4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 4(Fuca1-6)GlcNAcb 6)GlcNAcbGlcNAcb1-4(NeuAca2-3/6Galb1-4GlcNAcb1-Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GalNAcb1-2Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-4(Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-2Mana1-3)(Fuca1-3GlcNAcb1-2Mana1-6)Manb1- 6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-GalNAcb1-4(Fuca1-2)GlcNAcb1-2Mana1-3(Galb1-2Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-4(Fuca1-2)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcbb GalNAca1-3(Fuca1-2)Galb1-4(Fuca1-3)GlcNAcb1-Fuca1-3GalNAcb1-3Galb1-4Galb1-3(NeuGca2-2Mana1-3(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-8NeuGca2-8NeuGca2-8NeuGca2-6)GalNAc 4(Fuca1-6)GlcNAcMana1-3(Gal[3ME]b1-6Gal[3ME]b1-3(Gal[3ME]b1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-6)GalNAcb1-4GlcNAcb1-2Mana1-6)(Xylb1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-2)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4Glcb1-1GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-3)(GlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-3)(GlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-GalNAcb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3)(GlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-3(GalNAcb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1- 6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc GalNAcb1-4GlcNAcb1-2Mana1-3(GalNAcb1-GalNAcb1-4(NeuGca2-3)GalNAcb1-4Galb1-3Galb1-4GlcNAcb1-2(GalNAcb1-4GlcNAcb1-6)Mana1-3(NeuAca2-8NeuAca2-8NeuAca2-6)GalNAca 6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-GlcNAcb1-4(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcGlcNAcb1-4(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3)GlcNAcb1-2Mana1-3)(GlcNAcb1-2Mana1- 4GlcNAcb 6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(NeuGca2-3/6Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-2Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-3)(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Gala1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcb GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-GalNAca1-3(Fuca1-2)Galb1-4GlcNAcb1-2Mana1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2Mana1-3(GalNAca1-3(Fuca1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2)Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Fuca1-GlcNAcb1-4(Fuca1-2Galb1-4GlcNAcb1-2Mana1-2Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Neua1-3Galb1-4GlcNAcb1-2Mana1-3(Neua1-Kdna1-3Galb1-4GlcNAcb1-2Mana1-3(Kdna1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc 4GlcNAcbNeuGca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-NeuGca2-3Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-4GlcNAcb1-3Galb1-6)Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1- 3GalNAc 3GalNAcNeuGca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-GlcNAcb1-4(GalNAc[4S]b1-4GlcNAcb1-2Mana1-3Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-3)(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1- 3GalNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAcb Galb1-4GlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Gala1-4GlcNAcb1-2Mana1-3(Gala1-4GlcNAcb1-2(Gala1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcbGalb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-6Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAca1-2(Galb1-4(Fuca1-3)GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3/6(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-2(Galb1-4GlcNAcb1-6)Mana1-6/3)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-Galb1-4GlcNAcb1-4Mana1-3(Galb1-4GlcNAcb1-3)GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 6)Manb1-4GlcNAcb1-4GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3)Manb1-3(Galb1-4GlcNAcb1-2Manb1-6)Manb1-3Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Galb1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Galb1-3GlcNAcb1-2Mana1-3(Galb1-3GlcNAcb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Gala1-2(Galb1-3GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc GlcNAca1-6Galb1-4GlcNAcb1-2Mana1-3(Gala1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcb Galb1-4GlcNAcb1-2(Galb1-3GlcNAcb1-4)Mana1-GlcNAcb1-4(Galb1-4GlcNAcb1-2(GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1- 4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAcb GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(Gala1-3Galb1-4GlcNAcb1-2Mana1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4(Fuca1-3)GlcNAc Galb1-3GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1- 4(Fuca1-6)GlcNAc4GlcNAcb1-4GlcNAcb Galb1-4GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4(Fuca1-6)GlcNAcb4GlcNAcb1-4GlcNAc GlcNAcb1-4(Gala1-3Galb1-4GlcNAcb1-2Mana1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1- 4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Gal[3S]b1-NeuAca2-6Galb1-4GlcNAc[6S]b1-2Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcGal[3S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Gal[3S]b1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAc 6)GlcNAcNeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1- GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-3(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1- 6GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 4GlcNAcb1-4(Fuca1-6)GlcNAcbGalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1- GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1- 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-Glca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 6)Manb1-4GlcNAcMana1-3Mana1-2Mana1-2(Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-3Mana1-2Mana1- 6)Mana1-6)Manb1-4GlcNAcMana1-3Mana1-2Mana1-2(Mana1-3Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1- 6)Manb1-4GlcNAcMana1-3Mana1-2Mana1-2(Mana1-3Mana1-Glca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-2(Mana1-6)Mana1-6)Mana1-3(Mana1-3(Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1- 6)Mana1-6)Manb1-4GlcNAc6)Manb1-3GlcNAc Glcb1-2Glcb1-2Glcb1-2Mana1-2Mana1-2Mana1-GlcNAcb1-4(Neua1-6Galb1-4GlcNAcb1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)Manb1-4GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-GlcNAcb1-4(Gala1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAca1-2(Galb1-4GlcNAcb1-6)Mana1-3)(Gala1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1- 6)Manb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1- 4GlcNAcb1-4GlcNAcb6)Manb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(Galb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-2(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-6)Mana1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1- 6)Manb1-4GlcNAc6)Manb1-4GlcNAc Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(Galb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-3Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1- 6)Manb1-4GlcNAc6)Manb1-4GlcNAc Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1- 6)Manb1-4GlcNAc6)Manb1-4GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2(Glcb1-4GlcNAcb1-6)Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1- 6)Manb1-4GlcNAcb6)Manb1-4GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-3Galb1-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Gal[3S]b1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)Manb1-4GlcNAc 6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2(GlcNAcb1-4)Mana1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-3)(GalNAcb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-2(GlcNAcb1-4)Mana1-3)(GlcNAcb1-2Mana1-3)(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2(Fuca1-2Galb1-3GlcNAcb1-GlcNAcb1-4(GalNAca1-3(Fuca1-2)Galb1- 4)Mana1-3)(GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2Mana1-3)(GlcNAcb1-2Mana1- 4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalNAcb1-4(NeuGca2-3)GalNAcb1-3Galb1-4Galb1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-3(NeuGca2-8NeuGca2-8NeuGca2-6)GalNAc4(NeuAca2-3)Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcNeuAca2-6Galb1-3GlcNAcb1-3(NeuAca2-6Galb1-Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3GlcNAcb1-6)Galb1-4GlcNAcb1-3(NeuAca2-3(Mana1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 6)GalNAc 4(Fuca1-6)GlcNAcNeuGca2-3/6Galb1-4GlcNAcb1-2(GlcNAcb1-GlcNAca1-6Galb1-4GlcNAcb1-2Mana1-3(GlcNAca1-4)Mana1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)Manb1-4GlcNAcb1-4GlcNAc4(Fuca1-6)GlcNAc GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2Mana1-3(GalNAcb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-2(GalNAcb1-4GlcNAcb1-6)Mana1-6)Manb1- 4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-3(GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-4)Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcGalNAcb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4)Mana1-3)(GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-3(GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-3(GlcNAcb1-GalNAc[3S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcb GalNAc[4S]b1-4GlcNAcb1-2Mana1-3(NeuAca2-Mana1-2Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3(Mana1-2Mana1-2Mana1-6)Mana1-6)Manb1- 4(Fuca1-6)GlcNAcb4GlcNAcb1-4GlcNAc Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1-2Mana1-3(Mana1-2Mana1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAcb Mana1-3Mana1-2Mana1-2(Mana1-2Mana1-GlcNAcb1-4(NeuAca2-8NeuAca2-3/6Galb1-4(Fuca1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-3)GlcNAcb1-2Mana1-3)(Mana1-6)Manb1- 6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc NeuAca2-3Galb1-3(Galb1-4(Fuca1-3)GlcNACb1-NeuAca2-3Galb1-3(Fuca1-2Galb1-3(Fuca1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(FuCa1-4)GlcNAcb1-3(Galb1-4GlcNAcb1-6)Galb1-4(Fuca1- 3)GlcNAcb1-6)GalNAc3)GlcNAcb1-6)GalNAc NeuAca2-3Galb1-3(Fuca1-2Galb1-3(Fuca1-Galb1-3(NeuAca2-2Galb1-4(Fuca1-3)GlcNAcb1-4)GlcNAcb1-3(Galb1-4(Fuca1-3)GlcNAcb1-6)Galb1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1- 4GlcNAcb1-6)GalNAc3)GlcNAcb1-6)GalNAc GlcNAcb1-4(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNACb1-4)Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-6)GalNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-3(Galb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1- 6)Manb1-4GlcNAcb1-4GlcNAc3Galb1-3GalNAc Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc GlcNAcb1-4(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-NeuGca2-8NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-4)Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNACb1- 4GlcNAcb1-4GlcNAcb 4GlcNAcGlcNAcb1-4(GalNAcb1-4(Fuca1-3)GlcNAcb1-GlcNAcb1-4(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3)(GalNAcb1-4(Fuca1-3)GlcNACb1-2Mana1-3)(GalNAcb1-4GlcNAcb1-2Mana1- 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNACGal[3ME]b1-3GalNAcb1-4GlcNAcb1-2Mana1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3(Gal[3ME]b1-3GalNAcb1-4GlcNAcb1-2Mana1-6Galb1-4GalNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 4GlcNACNeuAca2-6Galb1-4GlcNAcb1-4Mana1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6(NeuAca2-6Galb1-4GlcNAcb1-4Mana1-6)Manb1-4GlcNAcb1-6GaFb1-4GlcNAcb1-2Manb1-3)Manb1-4GlcNAcb1- 4GlcNAcb 4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-4Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcNeuAca2-3Galb1-4GlcNAca1-2Mana1-3(NeuAca2-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAca1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 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4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3(Fuca1-Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-3(Fuca1-2Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcb4GlcNAcb1-4(Fuca1-6)GlcNAcb Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-3(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-3Galb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcb4GlcNAcb1-4(Fuca1-6)GlcNAc GlcNAcb1-3Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-GalNAcb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-3(GlcNAcb1-2(GlcNAcb1-6)Mana1-6)Manb1-2(GalNAcb1-4GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc GalNAcb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3(GalNAcb1-4GlcNAcb1-2Mana1-2(GlcNAcb1-4)Mana1-3)(GlcNAcb1-2(GlcNAcb1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-2(GlcNAcb1-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-4)Mana1-3)(GlcNAcb1-2(GlcNAcb1-6)Mana1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 4GlcNAcNeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-GlcNAcb1-4(NeuGca2-8NeuGca2-3/6Galb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb1-2Mana1-3)(Mana1-6)Manb1- 4GlcNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(NeuAca2-8NeuGca2-3/6Galb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuGca2-4GlcNAcb1-2Mana1-3)(Mana1-3Mana1-6)Manb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4GlcNAc 4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Gala1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(FuCa1-6)GlcNAc GlcNAcb1-4(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Gala1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcb NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-GlcNAcb1-4(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3)(Mana1-3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-Mana1-2Mana1-6(Mana1-2(ManaAll)Man[6P]a1-4GlcNAcb1-4)Mana1-3(Mana1-3Mana1-6)Manb1-2)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1- 4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAc Mana1-2Mana1-2(Mana1-2Mana1-6)Mana1-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuGca2-3(Mana1-3(Mana1-2(ManaAll)Man[6P]a1-6)Mana1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)Manb1-4GlcNAc 4GlcNAcbNeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuGca2-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuGca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAc 4GlcNAcNeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Gala1-NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Gala1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAcb NeuGca2-6Galb1-4GlcNAcb1-2Mana1-3(Galb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1- NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-NeuAca2-3GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-3Galb1-3GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc NeuAca2-6Galb1-4GlcNAcb1-2Mana1-NeuAc[4T]a1-6Galb1-4GlcNAcb1-2Mana1-3(NeuAc[4T]a1-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1- 6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc 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GlcNAcb1-4(Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-Kdna1-3Galb1-4GlcNAcb1-2Mana1-3(Kdna1-2Mana1-3)(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 6)Manb1-4GlcNAcb1-4GlcNAc4(Fuca1-6)GlcNAcb Gala1-3Galb1-4GlcNAcb1-2(Gala1-3Galb1-GlcNAcb1-3Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-4GlcNAcb1-4)Mana1-3(Mana1-3(Mana1-6)Mana1-3(GalNAcb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1- 6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-4)Mana1-3)(GlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-3)(Galb1-4GlcNAcb1-2(GlcNAcb1-4)(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGlcNAcb1-4(GlcNAcb1-2(GlcNAcb1-4)Mana1-NeuAca2-3Galb1-4GlcNAc[6S]b1-3Galb1-3)(GlcNAcb1-2(Galb1-4GlcNAcb1-4)(GlcNAcb1-4GlcNAc[6S]b1-3Galb1-4GlcNAcb1-3Galb1- 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-3Galb1-3GalNAc GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-3)(NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-6)Manb1-4GlcNAcb1-4GlcNAc-4GlcNAc 4GlcNAcb1-4GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-6Galb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2(Galb1-3(NeuAca2-6)GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-4GlcNAcb1-4)Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcbGalb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAcb Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-6)Manb1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2Mana1- 4GlcNAcb1-4(Fuca1-6)GlcNAcb6)Manb1-4GlcNAcb1-4GlcNAc Galb1-4GlcNAcb1-2Mana1-3(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-2(Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-3)GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2Mana1-3(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-3(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcb4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3(Galb1-4GlcNacb1-2Mana1-6)Manb1-2(Galb1-4GlcNAcb1-4)Mana1-3)(Mana1-3Mana1- 4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-2(GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1-6Galb1-4GlcNAc[6S]b1-2Mana1-6)Manb1- 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4GlcNAc GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-3GalNAcb1-4GlcNAcb1-2Mana1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbNeuAc[4T]a1-6Galb1-4GlcNAcb1-2Mana1-NeuGca2-3Galb1-4GlcNAc[6S]b1-3Galb1-3(NeuAc[4T]a1-6Galb1-4GlcNAcb1-2Mana1-4GlcNAc[6S]b1-3Galb1-4GlcNAcb1-3Galb1- 6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-3Galb1-3GalNAc 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6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(Fuca1-2Galb1-4(Fuca1-3)GlcNAcb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-2Mana1-3)(GalNAcb1-4(Fuca1-3)GlcNAcb1-3)(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1- 2Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc Mana1-2Mana1-2(Mana1-2(Mana1-2(Mana1-Mana1-3Mana1-2Mana1-2Mana1-3(Mana1-6)Mana1-6)Mana1-6)Mana1-3(Mana1-3(Mana1-3(Mana1-3Mana1-2(Mana1-3Mana1-2Mana1- 2Mana1-6)Mana1-6)Manb1-4GlcNAc6)Mana1-6)Mana1-6)Manb1-4GlcNAcGlca1-2Glca1-3Glca1-3Mana1-2Mana1-2(Mana1-Glca1-2Glca1-3Glca1-3Mana1-2Mana1-2(Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-2Mana1-6)Mana1-3(Mana1-3(Mana1-3Mana1-2Mana1- 6)Mana1-6)Manb1-4GlcNAc6)Mana1-6)Manb1-4GlcNAc Mana1-2Mana1-2(Mana1-2(Mana1-6Mana1-Mana1-2Mana1-2Mana1-3(Mana1-3Mana1-6Mana1-6)Mana1-6)Mana1-3(Mana1-3(Mana1-3(Mana1-3Mana1-2(Mana1-3Mana1-2Mana1- 2Mana1-6)Mana1-6)Manb1-4GlcNAc6)Mana1-6)Mana1-6)Manb1-4GlcNAc 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6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGlcNAcb1-4(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-Galb1-4GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-4)Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-GlcNAcb1-4(Galb1-4GlcNAcb1-2Mana1-3)(Galb1-3(Galb1-4GlcNAcb1-2(GlcNAcb1-6)Mana1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3)(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-Glca1-3Glca1-3Glca1-3Mana1-2Mana1-2Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1- 6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc Glca1-2Glca1-3Glca1-3Mana1-2Mana1-2Mana1-Mana1-3Mana1-2Mana1-2Mana1-3(Mana1-3(Mana1-2Mana1-3(Mana1-2Mana1-6)Mana1-3(Mana1-3Mana1-2(Mana1-2Mana1-6)Mana1- 6)Manb1-4GlcNAcb1-4GlcNAcb6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbNeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc NeuAca2-3Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-4GlcNAcb1-4)Mana1-3(Mana1-6)Manb1-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAcb NeuAca2-3Galb1-4GlcNAca1-2Mana1-3(NeuAca2-NeuAca2-6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-4GlcNAca1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAc4(Fuca1-6)GlcNAc NeuAca2-3/6Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-NeuAca2-3Galb1-4GlcNAcb1-2Mana1-3(NeuAca2-3/6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1- 4(Fuca1-6)GlcNAcb4(Fuca1-6)GlcNAc 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6)Manb1-4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2Mana1-GlcNAcb1-4(NeuAca2-3/6Galb1-4(Fuca1-3(GalNAcb1-4(Fuca1-3)GlcNAcb1-2Mana1-3)GlcNAcb1-2Mana1-3)(Fuca1-3GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(Galb1-4GlcNAcb1-2(GlcNAcb1-GalNAcb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3)(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGala1-3Galb1-4GlcNAcb1-2Mana1-3(NeuGca2-GlcNAcb1-4(NeuGca2-8NeuGca2-3/6Galb1-8NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1-6)Manb1-4GlcNAcb1-2Mana1-3)(Mana1-3(Mana1-6)Mana1- 4GlcNAcb1-4GlcNAc6)Manb1-4GlcNAcb1-4GlcNAc NeuAca2-3/6Galb1-4GlcNAcb1-2(Gala1-3Galb1-NeuGca2-3/6Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4GlcNAcb1-4)Mana1-3(Mana1-3(Mana1-6)Mana1-4)Mana1-3(Mana1-3(Mana1-6)Mana1-6)Manb1- 6)Manb1-4GlcNAcb1-4GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc 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6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-6Galb1-4GlcNAc[6S]b1-2Mana1-NeuAca2-6Galb1-4GlcNAc[6S]b1-2Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc NeuAca2-3GalNAcb1-4GlcNAcb1-2Mana1-NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-3GalNAcb1-4GlcNAcb1-2Mana1-3(NeuAca2-6GalNAcb1-4GlcNAcb1-2Mana1- 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcb GalNAca1-3(Fuca1-2)Galb1-3GlcNAcb1-NeuAca2-3GalNAcb1-4GlcNAcb1-2Mana1-3(GalNAca1-3(NeuAca2-6)Galb1-3GlcNAcb1-3(NeuAca2-3GalNAcb1-4GlcNAcb1-2Mana1-6)Galb1-4GlcNAcb1-3(NeuAca2-6)GalNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbGalb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(GlcNAcb1-GlcNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-4)Mana1-3(GalNAcb1-4GlcNAcb1-2(GlcNAcb1-3Galb1-4GlcNAcb1-2(GlcNAcb1-3Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 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6)Manb1-4GlcNAcb1-4GlcNAc3(Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcNeuGca2-3/6Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(Gala1-3Galb1-4GlcNAcb1-2Mana1-4)Mana1-3(Galb1-4GlcNAcb1-2Mana1-3)Manb1-3)(NeuGca2-3/6Galb1-4GlcNAcb1-2Mana1- 4GlcNAcb1-4(Fuca1-6)GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-6Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4)Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4GlcNAcb1-4)Mana1-3)(Mana1-3(Mana1-6)Mana1- 6)Mana1-6)Manb1-4GlcNAc6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc NeuAca2-6Galb1-4GlcNAc[6S]b1-2Mana1-3(NeuGca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAcNeuGca2-6Galb1-4GlcNAc[6S]b1-2Mana1-NeuGca2-6Galb1-4GlcNAc[6S]b1-2Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-4(Fuca1-6)GlcNAc 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6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-3Galb1-GlcNAcb1-4(GlcNAcb1-3Galb1-4GlcNAcb1-4GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2(Galb1-2(GlcNAcb1-4)Mana1-3)(GalNAcb1-4GlcNAcb1-4GlcNAcb1-6)Mana1-6)Manb1-4Glcb2(GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcGalNAcb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-NeuGca2-8NeuGca2-3/6Galb1-4GlcNAcb1-4)Mana1-3(GalNAcb1-4GlcNAcb1-2(GalNAcb1-2(GlcNAcb1-4)Mana1-3(GlcNAcb1-2(GlcNAcb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc NeuAca2-3/6Galb1-4GlcNAcb1-2(GlcNAcb1-GlcNAcb1-4(Galb1-4(Fuca1-3)GlcNAcb1-2(Galb1-4)Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-4GlcNAcb1-4)Mana1-3)(Galb1-4GlcNAcb1-2Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGalb1-4(Fuca1-3)GlcNAcb1-2(GlcNAcb1-4)Mana1-Galb1-4(Fuca1-3)GlcNAcb1-2(GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-3(Galb1-4GlcNAcb1-2(Galb1-4GlcNAcb1-6)Mana1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuGca2-8NeuGca2-3/6Galb1-4(Fuca1-NeuAca2-4Galb1-3(NeuAca2-6)GlcNAcb1-2Mana1-3)GlcNAcb1-2Mana1-3(Mana1-3(Mana1-6)Mana1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc 4GlcNAcb1-4GlcNAcNeuAca2-4Galb1-3(NeuAca2-6)GlcNAcb1-2Mana1-NeuAca2-3Galb1-3(NeuAca2-6)GlcNAcb1-2Mana1-3(NeuAca2-4Galb1-3GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-6Galb1-3GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAcb4GlcNAcb1-4GlcNAc NeuAca2-3Galb1-3(NeuAca2-6)GlcNAcb1-2Mana1-NeuAca2-3Galb1-3(NeuAca2-6)GlcNAcb1-2Glca1-3(NeuAca2-6Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-6Galb1-4GlcNAcb1-2Glca1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAcb NeuAca2-8NeuAca2-3/6Galb1-4GlcNAcb1-2Mana1-NeuAca2-3Galb1-3(NeuAca2-6)GlcNAcb1-2Mana1-3(NeuAca2-3/6Galb1-4GlcNAcb1-2Mana1-6)Manb1-3(NeuAca2-3Galb1-4GlcNAcb1-2Mana1-6)Manb1- 4GlcNAcb1-4GlcNAc4GlcNAcb1-4GlcNAcb NeuAca2-3Galb1-3(NeuAca2-6)GlcNAcb1-2Mana1-3(NeuAca2-3Galb1-3GlcNAcb1-2Mana1-6)Manb1 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2(NeuAca2-3Galb1-4GlcNAcb1-4)Mana1-3(NeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3(NeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcbNeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3(NeuAca2-8NeuAca2-3/6Galb1-4)Mana1-3(NeuAca2-8NeuAca2-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1- 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc 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6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3(NeuAca2-8NeuAca2-3/6Galb1-4)Mana1-3(NeuAca2-8NeuAca2-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcNeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-GlcNAcb1-4(NeuAca2-3/6Galb1-4(Fuca1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-4)Mana1-3(NeuAca2-8NeuGca2-3/6Galb1-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuAca2-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-GlcNAcb1-4(NeuAca2-3/6Galb1-4(Fuca1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-4)Mana1-3(NeuGca2-8NeuGca2-3/6Galb1-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuAca2-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-4)Mana1-3(NeuGca2-8NeuGca2-3/6Galb1-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuAca2-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuGca2-3)GlcNAcb1-4)Mana1-3)(NeuGca2-8NeuGca2-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1- 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-GlcNAcb1-4(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3)(NeuGca2-8NeuGca2-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuAca2-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1- 6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(NeuAca2-3/6Galb1-4(Fuca1-GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuAca2-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuAca2-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-GlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3)(NeuAca2-8NeuGca2-3)GlcNAcb1-4)Mana1-3)(NeuGca2-8NeuGca2-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-2(NeuAca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAcGlcNAcb1-4(NeuGca2-3/6Galb1-4(Fuca1-Fuca1-3GalNAcb1-3Gala1-3Galb1-4GlcNAcb1-3)GlcNAcb1-2(NeuGca2-3/6Galb1-4(Fuca1-2(Fuca1-3GalNAcb1-3Gala1-3Galb1-4GlcNAcb1-3)GlcNAcb1-4)Mana1-3)(NeuGca2-8NeuGca2-4)Mana1-3(Fuca1-3GalNAcb1-3Gala1-3Galb1-3/6Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-4GlcNAcb1-2(Fuca1-3GalNAcb1-3Gala1-3Galb1-2(NeuGca2-3/6Galb1-4(Fuca1-3)GlcNAcb1-4GlcNAcb1-4)(Fuca1-3GalNAcb1-3Gala1-3Galb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-6)GlcNAc4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcbFuca1-3GalNAcb1-3Gala1-3Galb1-4GlcNAcb1-NeuAca2-6Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(Fuca1-3GalNAcb1-3Gala1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-4)(Fuca1-3GalNAcb1-3Gala1-3Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-6)Mana1-3(Fuca1-3GalNAcb1-3Gala1-3Galb1-3)GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(Fuca1-3GalNAcb1-3Gala1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-4GlcNAcb1-4)Mana1-6)Manb1-4GlcNAcb1-4GlcNAcb3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1- 6)GlcNAcbNeuAca2-6Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-NeuAca2-6Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3(Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4GlcNAcb1-2(Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-3Galb1-3)GlcNAcb1-4)Mana1-3(Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-4GlcNAcb1-3Galb1-4GlcNAcb1-2(NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-3Galb1-4(Fuca1-3)GlcNAcb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1-4(Fuca1-3Galb1-4GlcNAcb1-6)Mana1-6)Manb1-4GlcNAcb1- 6)GlcNAcb 4(Fuca1-6)GlcNAcbReferences

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All patents and publications referenced or mentioned herein areindicative of the levels of skill of those skilled in the art to whichthe invention pertains, and each such referenced patent or publicationis hereby incorporated by reference to the same extent as if it had beenincorporated by reference in its entirety individually or set forthherein in its entirety. Applicants reserve the right to physicallyincorporate into this specification any and all materials andinformation from any such cited patents or publications.

The specific methods and compositions described herein arerepresentative of preferred embodiments and are exemplary and notintended as limitations on the scope of the invention. Other objects,aspects, and embodiments will occur to those skilled in the art uponconsideration of this specification, and are encompassed within thespirit of the invention as defined by the scope of the claims. It willbe readily apparent to one skilled in the art that varying substitutionsand modifications may be made to the invention disclosed herein withoutdeparting from the scope and spirit of the invention. The inventionillustratively described herein suitably may be practiced in the absenceof any element or elements, or limitation or limitations, which is notspecifically disclosed herein as essential. The methods and processesillustratively described herein suitably may be practiced in differingorders of steps, and that they are not necessarily restricted to theorders of steps indicated herein or in the claims. As used herein and inthe appended claims, the singular forms “a,” “an,” and “the” includeplural reference unless the context clearly dictates otherwise. Thus,for example, a reference to “a host cell” includes a plurality (forexample, a culture or population) of such host cells, and so forth.Under no circumstances may the patent be interpreted to be limited tothe specific examples or embodiments or methods specifically disclosedherein. Under no circumstances may the patent be interpreted to belimited by any statement made by any Examiner or any other official oremployee of the Patent and Trademark Office unless such statement isspecifically and without qualification or reservation expressly adoptedin a responsive writing by Applicants.

The terms and expressions that have been employed are used as terms ofdescription and not of limitation, and there is no intent in the use ofsuch terms and expressions to exclude any equivalent of the featuresshown and described or portions thereof, but it is recognized thatvarious modifications are possible within the scope of the invention asclaimed. Thus, it will be understood that although the present inventionhas been specifically disclosed by preferred embodiments and optionalfeatures, modification and variation of the concepts herein disclosedmay be resorted to by those skilled in the art, and that suchmodifications and variations are considered to be within the scope ofthis invention as defined by the appended claims.

The invention has been described broadly and generically herein. Each ofthe narrower species and subgeneric groupings falling within the genericdisclosure also form part of the invention. This includes the genericdescription of the invention with a proviso or negative limitationremoving any subject matter from the genus, regardless of whether or notthe excised material is specifically recited herein.

Other embodiments are within the following claims. In addition, wherefeatures or aspects of the invention are described in terms of Markushgroups, those skilled in the art will recognize that the invention isalso thereby described in terms of any individual member or subgroup ofmembers of the Markush group.

1. An array of glycan molecules comprising a solid support and a libraryof glycan molecules, wherein each glycan molecule is covalently attachedto the solid support via amide or amine group.
 2. The array of claim 1,wherein each type of glycan molecule in the library is attached to thesolid support at a defined glycan probe location.
 3. The array of claim2, wherein each glycan probe location defines a region of the solidsupport that has multiple copies of one type of similar glycan moleculesattached thereto.
 4. The array of claim 1, wherein the array is amicroarray.
 5. The array of claim 1, wherein the solid support is aglass slide.
 6. The array of claim 1, wherein the glass slide is coatedwith a hydrogel.
 7. The array of claim 1, wherein the glycan moleculesare printed onto the solid support.
 8. The array of claim 1, wherein theglycan molecules are printed onto an amino-reactive solid support. 9.The array of claim 1, wherein the glycan molecules are printed onto anN-hydroxysuccinimide (NHS)-derivatized solid support.
 10. The array ofclaim 9, wherein each glycan molecule in the library is attached to thesolid support via an amino acid that forms a linkage to theN-hydroxysuccinimide (NHS)-derivatized solid support.
 11. The array ofclaim 1, wherein each glycan is covalently attached to a spacer, whichis attached to the solid support by the amide linkage.
 12. The array ofclaim 11, wherein each glycan is covalently attached to a spacer by anether, an ester, an amide or a combination thereof.
 13. The array ofclaim 11, wherein the spacer is an alkyl, a peptide, an amino acid, aprotein or a combination thereof.
 14. The array of claim 1, wherein eachglycan molecule in the library is attached directly to the solidsupport.
 15. The array of claim 1, comprising 10-100,000 separate,isolated glycans, wherein the glycans are straight or branched chains ofallose, altrose, arabinose, glucose, galactose, gulose, fucose,fructose, idose, lyxose, mannose, ribose, talose, or xylose sugar unitscovalently linked together by alpha (α) or beta (β) covalent linkages;and the sugar units can have N-acetyl, N-acetylneuraminic acid, oxy(═O), sialic acid, sulfate (—SO₄ ⁻), phosphate (—PO₄ ⁻), lower alkoxy,lower alkanoyloxy, lower acyl, and/or lower alkanoylaminoalkylsubstituents that are present instead of, or in addition to, hydroxy(—OH), carboxylic acid (—COOH) and methylenehydroxy (—CH₂—OH)substituents present on the sugar units.
 16. The array of claim 1,wherein a portion of the glycans are naturally occurring glycans. 17.The array of claim 1, wherein a portion the glycans are enzymaticallysynthesized glycans.
 18. The array of claim 1, wherein the glycanscomprise glycoamino acids, glycopeptides, glycolipids,glycoaminoglycans, glycoproteins, cellular components, glycoconjugates,glycomimetics, glycophospholipids, glycosyl phosphatidylinositol-linkedglycoconjugates, bacterial lipopolysaccharides or a combination thereof.19. The array of claim 1, wherein at least one glycan comprises analpha-Gal-3 glycan, an alpha-Gal-LeX glycan, a Fucα1-3GlcNAc glycan, aFucα1-4GlcNAc glycan, a Siaα2-6Galβ1-4GlcNAc glycan, aNeu5Acα2-6Galβ1-4GlcNAc[6Su] glycan, a Lewis^(x)(Galβ1-4[Fucα1-3]GlcNAc) glycan, a Neu5Acα2-3-galactoside, aNeu5Acα2-6-sialoside, a Neu5Acα2-8-sialoside or a combination thereof.20. The array of claim 1, wherein the library of glycans furthercomprises at least thirty five glycans selected from Table 3 or Table 9provided herein.
 21. A library comprising 225-7500 separate, isolatedglycans, selected from the glycans listed in Table 3 or Table 9 providedherein.
 22. The library of claim 21, wherein each glycan in the array iscovalently attached to a spacer.
 23. The library of claim 21, whereinthe spacer is an alkyl, a peptide, an amino acid, a protein or acombination thereof.
 24. The library of claim 22, wherein the spacer isan aminoalkyl.
 25. The library of claim 21, wherein each glycan iscovalently attached to an amino acid.
 26. A composition comprising acarrier and an effective amount of at least one glycan molecule, whereineach glycan molecule in the composition binds an antibody found in apatient with a disease, and wherein serum from a patient without thedisease has substantially no antibodies that bind any of the glycanmolecules in the composition.
 27. The composition of claim 26, whereinthe disease is a bacterial infection, viral infection, inflammation,cancer, transplant rejection, or an autoimmune disease.
 28. Thecomposition of claim 26, which has at least two glycan molecules. 29.The composition of claim 26, which is formulated for immunization of amammal.
 30. The composition of claim 26, which is formulated for localadministration to a tissue.
 31. The composition of claim 26, which isformulated as a food supplement.
 32. The composition of claim 26,wherein the at least one glycan is selected from glycans listed in Table3 or Table 9 provided herein.
 33. A composition comprising a carrier andan effective amount of an alpha-Gal-3 glycan, wherein the composition isformulated for treating or preventing transplant tissue rejection. 34.The composition of claim 33, wherein the alpha-Gal-3 glycan isGal-alpha3-Gal-beta (structure 33),Gal-alpha3-Gal-beta4-GlcNAc[alpha3-Fucose]-beta (structure 34),Gal-alpha3-Gal-beta4-Glc-beta (structure 35),Gal-alpha3-Gal[alpha2-Fucose]-beta4-GlcNAc-beta (structure 36),Gal-alpha3-Gal-beta4-GalAc-beta (structure 37), Gal-alpha3-GalAc-alpha(structure 38), Gal-alpha3-Gal-beta (structure 39) or a combinationthereof.
 35. A composition comprising a carrier and an effective amountof at least one glycan molecule, wherein each glycan molecule in thecomposition binds an antibody found in a healthy person, and whereinserum from a patient with the disease has substantially no antibodiesthat bind any of the glycan molecules in the composition.
 36. A methodof testing whether a molecule in a test sample can bind to a glycancomprising, (a) contacting glycans in the array of claim 1 with the testsample, and (b) observing whether a molecule in the test sample binds toa glycan in the array.
 37. The method of claim 36, wherein the methodfurther comprises determining which molecule in the test sample binds tothe glycan.
 38. The method of claim 36, wherein the molecule is anantibody, an enzyme, a viral protein, a cellular receptor, a cell typespecific antigen, or a nucleic acid, a cellular component or a tissuecomponent.
 39. The method of claim 38, wherein the nucleic acid is RNA.40. The method of claim 36, wherein the molecule is from a prokaryote,prion, virus, bacterium or eukaryote.
 41. A method of testing whether amolecule in a test sample can bind to a glycan comprising, (a)contacting glycans in the library of claim 21 with the test sample and(b) observing whether a molecule in the test sample binds to a glycan inthe library.
 42. The method of claim 41, wherein the method furthercomprises determining which molecule in the test sample binds to theglycan.
 43. The method of claim 41, wherein the molecule is an antibody,an enzyme, a viral protein, a cellular receptor, a cell type specificantigen, or a nucleic acid, a cellular component or a tissue component.44. The method of claim 43, wherein the nucleic acid is RNA.
 45. Themethod of claim 41, wherein the molecule is from a prokaryote, prion,virus, bacterium or eukaryote.
 46. A method of detecting antibodies in atest sample comprising contacting the test sample with the array ofclaim 1 and observing whether one or more glycans are bound by anantibody in the test sample.
 47. The method of claim 46, wherein thetest sample is blood, serum, anti-serum, monoclonal antibodypreparation, lymph, plasma, saliva, urine, semen, breast milk, ascitesfluid, tissue extract, cell lysate, cell suspension, viral suspension,or a combination thereof.
 48. The method of claim 46, which furthercomprises observing whether antibodies in a control sample bind to thesame glycan molecules as are bound by the antibodies in the test sample.49. A method of detecting antibodies in a serum comprising contactingthe serum with the array of claim 1 and observing whether one or moreglycans are bound by antibodies.
 50. A method of detecting transplanttissue rejection in a transplant recipient comprising contacting a testsample from the transplant recipient with an array of glycans andobserving whether one or more glycans are bound by antibodies in thetest sample.
 51. A method of detecting xenotransplant tissue rejectionin a transplant recipient comprising contacting a test sample from thetransplant recipient with an array of glycans and observing whether oneor more glycans are bound by antibodies in the test sample, wherein theglycans in the array include any one of Gal-alpha3-Gal-beta (structure33 of FIG. 7), Gal-alpha3-Gal-beta4-GlcNAc[alpha3-Fucose]-beta(structure 34 of FIG. 7), Gal-alpha3-Gal-beta4-Glc-beta (structure 35 ofFIG. 7), Gal-alpha3-Gal[alpha2-Fucose]-beta4-GlcNAc-beta (structure 36of FIG. 7), Gal-alpha3-Gal-beta4-GalAc-beta (structure 37 of FIG. 7),Gal-alpha3-GalAc-alpha (structure 38 of FIG. 7), Gal-alpha3-Gal-beta(structure 39 of FIG. 7), or Gal-beta4-GlcNAc[alpha3-Fucose]-beta(structure 65 in FIG. 7) or a combination thereof.
 52. The method ofclaim 51, wherein the test sample is blood, serum, plasma, saliva,urine, breast milk, ascites fluid or lymph.
 53. The method of claim 51,wherein at least one glycan comprises alpha-Gal-LeX(Gal-alpha3-Gal-beta4-GlcNAc[alpha3-Fucose]-beta (structure 34 in FIG.7), which is not found in humans, but which is present on porcine cells.54. A method of treating or preventing disease in a mammal thatcomprises administering to the mammal a composition comprising aneffective amount of at least one glycan molecule that binds antibodiesdetected in a patient with the disease.
 55. The method of claim 54,wherein the at least one glycan comprises an alpha-Gal-3 glycan or analpha-Gal-LeX glycan.
 56. An isolated antibody that can bind analpha-Gal-3 glycan.
 57. An isolated antibody that can bind a glycan thatcomprises Gal-alpha3-Gal-beta (structure 33 of FIG. 7),Gal-alpha3-Gal-beta4-GlcNAc[alpha3-Fucose]-beta (structure 34 of FIG.7), Gal-alpha3-Gal-beta4-Glc-beta (structure 35 of FIG. 7),Gal-alpha3-Gal[alpha2-Fucose]-beta4-GlcNAc-beta (structure 36 of FIG.7), Gal-alpha3-Gal-beta4-GalAc-beta (structure 37 of FIG. 7),Gal-alpha3-GalAc-alpha (structure 38 of FIG. 7), Gal-alpha3-Gal-beta(structure 39 of FIG. 7) or a combination thereof.
 58. A kit comprisingthe array of claim 1 and instructions for using the array.
 59. A kitcomprising the library of glycans of claim 21 and instructions formaking an array from the library of glycans.
 60. The kit of claim 59,further comprising a solid support for making the array.